- phenixbb - phenix-online.org

Workshop on nMX at ECM31, the programme now online
by John R Helliwell 02 Aug '18

02 Aug '18

Dear Colleagues, The Workshop on nMX at ECM31, the programme is now online at:- https://ecm31.ecanews.org/en/neutron-macromolecular-crystallography.php There is still time to register. Best wishes, John Emeritus Professor John R Helliwell DSc

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Error building Amber interface to phenix
by Roger Shek 30 Jul '18

30 Jul '18

I am trying to build the amber interface to phenix, but encounter an error. Running OpenSUSE15. Anyone have any ideas? phenix.build_amber_interface Phenix modules found : /opt/phenix-1.13-2998/modules/phenix $AMBERHOME set : /home/roger/bin/Amber/amber18 Linking AMBERHOME to Phenix modules Not linking $AMBERHOME into Phenix modules directory because there is already a link and it points to the same directory as $AMBERHOME. $AMBERHOME : /home/roger/bin/Amber/amber18 Phenix link: /opt/phenix-1.13-2998/modules/amber Building amber_adaptbx ~> libtbx.configure amber Python: 2.7.14 "/opt/phenix-1.13-2998/base/bin/python2.7" Compiler: default Build mode: release Warning level: 0 Precompiled Headers: False Static libraries: False Static exe: False Scan Boost headers: False Write full flex_fwd.h files: False Build Boost.Python extensions: True Define BOOST_PYTHON_NO_PY_SIGNATURES: False Define BOOST_PYTHON_BOOL_INT_STRICT: True Enable OpenMP if possible: False Boost threads enabled: False Enable CUDA: False Use opt_resources if available: False Use environment flags: False Enable C++11: False Python3 migration warning policy: None command_version_suffix: 1.13-2998 Relocatable paths anchored at: /opt/phenix-1.13-2998/build Top-down list of all modules involved: prime "/opt/phenix-1.13-2998/modules/cctbx_project/prime" iota "/opt/phenix-1.13-2998/modules/cctbx_project/iota" xia2 "/opt/phenix-1.13-2998/modules/xia2" xfel "/opt/phenix-1.13-2998/modules/cctbx_project/xfel" dials "/opt/phenix-1.13-2998/modules/dials" simtbx "/opt/phenix-1.13-2998/modules/cctbx_project/simtbx" cma_es "/opt/phenix-1.13-2998/modules/cctbx_project/cma_es" labelit "/opt/phenix-1.13-2998/modules/labelit" rstbx "/opt/phenix-1.13-2998/modules/cctbx_project/rstbx" spotfinder "/opt/phenix-1.13-2998/modules/cctbx_project/spotfinder" annlib+adaptbx "/opt/phenix-1.13-2998/modules/annlib" "/opt/phenix-1.13-2998/modules/annlib_adaptbx" phenix "/opt/phenix-1.13-2998/modules/phenix" reel "/opt/phenix-1.13-2998/modules/reel" wxtbx "/opt/phenix-1.13-2998/modules/cctbx_project/wxtbx" phaser_regression "/opt/phenix-1.13-2998/modules/phaser_regression" phaser "/opt/phenix-1.13-2998/modules/phaser" tntbx "/opt/phenix-1.13-2998/modules/tntbx" solve_resolve "/opt/phenix-1.13-2998/modules/solve_resolve" muscle "/opt/phenix-1.13-2998/modules/muscle" ksdssp "/opt/phenix-1.13-2998/modules/ksdssp" pulchra "/opt/phenix-1.13-2998/modules/pulchra" phenix_html "/opt/phenix-1.13-2998/modules/phenix_html" phenix_regression "/opt/phenix-1.13-2998/modules/phenix_regression" elbow "/opt/phenix-1.13-2998/modules/elbow" Plex "/opt/phenix-1.13-2998/modules/Plex" PyQuante "/opt/phenix-1.13-2998/modules/PyQuante" crys3d "/opt/phenix-1.13-2998/modules/cctbx_project/crys3d" gltbx "/opt/phenix-1.13-2998/modules/cctbx_project/gltbx" amber+adaptbx "/opt/phenix-1.13-2998/modules/amber" "/opt/phenix-1.13-2998/modules/amber_adaptbx" mmtbx "/opt/phenix-1.13-2998/modules/cctbx_project/mmtbx" suitename "/opt/phenix-1.13-2998/modules/suitename" king "/opt/phenix-1.13-2998/modules/king" probe "/opt/phenix-1.13-2998/modules/probe" reduce "/opt/phenix-1.13-2998/modules/reduce" iotbx "/opt/phenix-1.13-2998/modules/cctbx_project/iotbx" ccp4io+adaptbx "/opt/phenix-1.13-2998/modules/ccp4io" "/opt/phenix-1.13-2998/modules/ccp4io_adaptbx" dxtbx "/opt/phenix-1.13-2998/modules/cctbx_project/dxtbx" cbflib+adaptbx "/opt/phenix-1.13-2998/modules/cbflib" "/opt/phenix-1.13-2998/modules/cctbx_project/cbflib_adaptbx" smtbx "/opt/phenix-1.13-2998/modules/cctbx_project/smtbx" ucif "/opt/phenix-1.13-2998/modules/cctbx_project/ucif" cctbx "/opt/phenix-1.13-2998/modules/cctbx_project/cctbx" scitbx "/opt/phenix-1.13-2998/modules/cctbx_project/scitbx" fable "/opt/phenix-1.13-2998/modules/cctbx_project/fable" omptbx "/opt/phenix-1.13-2998/modules/cctbx_project/omptbx" boost+adaptbx "/opt/phenix-1.13-2998/modules/boost" "/opt/phenix-1.13-2998/modules/cctbx_project/boost_adaptbx" tbxx "/opt/phenix-1.13-2998/modules/cctbx_project/tbxx" chiltbx "/opt/phenix-1.13-2998/modules/cctbx_project/chiltbx" libtbx "/opt/phenix-1.13-2998/modules/cctbx_project/libtbx" Processing: "/opt/phenix-1.13-2998/build/dispatcher_include_amber.sh" Processing: "/opt/phenix-1.13-2998/build/dispatcher_include_phenix.sh" Creating files in build directory: "/opt/phenix-1.13-2998/build" dispatcher_include_template.sh dispatcher_head.sh Traceback (most recent call last): File "/opt/phenix-1.13-2998/modules/cctbx_project/libtbx/env_config.py", line 2462, in <module> warm_start(sys.argv) File "/opt/phenix-1.13-2998/modules/cctbx_project/libtbx/env_config.py", line 2456, in warm_start env.refresh() File "/opt/phenix-1.13-2998/modules/cctbx_project/libtbx/env_config.py", line 1615, in refresh self.write_lib_dispatcher_head() File "/opt/phenix-1.13-2998/modules/cctbx_project/libtbx/env_config.py", line 1248, in write_lib_disp atcher_head target_file=self.under_build(target_file, return_relocatable_path=True)) File "/opt/phenix-1.13-2998/modules/cctbx_project/libtbx/env_config.py", line 1146, in write_bin_sh_d ispatcher target_file.chmod(0755) File "/opt/phenix-1.13-2998/modules/cctbx_project/libtbx/path.py", line 279, in chmod return os.chmod(abs(self), *args, **kwds) OSError: [Errno 1] Operation not permitted: '/opt/phenix-1.13-2998/build/dispatcher_head.sh' -- Roger Shek Stony Brook University Graduate Student in Biochemistry and Structural Biology (PhD) Stony Brook Integrative Structural Biology Organization <http://sbinststrbio.com/> Cell: (808) 386-3879 Website: https://www.rogershek.com

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Ligand occupancy and conformational change
by Xavier Brazzolotto 24 Jul '18

24 Jul '18

I am struggling with a ligand bound structure. The ligand seems to induce a small conformational change of one loop. However, despite my efforts I did not get any data with a full occupancy for this ligand yet. As a result, I have to deal with a loop in apo state (where ligand occupancy = 0) and a loop with a bound ligand (where ligand occupancy <1) and where the ligand is clashing with the modelled loop in the apo state. Hope I did myself clear. How to deal with this situation ? I am sure that phenix.refine can do it but how ? What I would like to try is something like that "alternate loop A" occupancy = X and "alternate loop B" occupancy = ligand occupancy = 1-X Maybe something specific in a parameter file ? Thank you for your help Xavier

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How to use phaser gyre and gimble in phenix
by Meinke, Gretchen 19 Jul '18

19 Jul '18

Hello again-- I have partially solved my silly problem: This is how to use it. phenix.gyre_and_gimble I may write back for more specifics, if my MR remains unsolved. Thanks! Gretchen

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How to use phaser gyre and gimble in phenix
by Meinke, Gretchen 18 Jul '18

18 Jul '18

Hi! I have a challenging MR problem and maybe phenix.phaser gyre and gimble will help. My molecule is flexible horsehoe shaped slinky, there are multiples in the unit cell (maybe 8-12??). My data is medium resolution 3.5 maybe. There are good homology models (also flexible!) It seems to have 1-2 hinge points (or 2-3 domains). I saw your publication "Gyre and gimble: a maximum-likelihood replacement for Patterson correlation refinement" Acta Cryst. (2018). D74, 279–289 and that describes exactly what I would like to do. One problem, I cannot at all figure out how to use gyre in gimble in phenix. I cannot find it in the GUI, and am unclear how to run it as a script. It looks super useful and would love to use it. Any help, a script, etc would be most appreciated! Thanks! Gretchen

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FW: Occupancy / alternate conformation Refinement
by Schulz, Eike-Christian 17 Jul '18

17 Jul '18

Dear all, In one of my structures I appear to have a mixed state between a covalently bound intermediate and the free substrate occupying _almost_ the same position. I can model the states nicely in coot, but during refinement the molecules “fly” apart - although the occupancy was limited to 0.5 for their overlapping atoms. I have tried to model the free ligand as an alternate conformation of the covalent intermediate: HETATM 852 N ASB A 110 10.523 15.702 10.022 1.00 14.48 N HETATM 853 CA ASB A 110 9.974 15.713 8.664 1.00 15.11 C HETATM 854 C ASB A 110 8.635 16.385 8.683 1.00 14.31 C HETATM 855 O ASB A 110 8.563 17.443 9.233 1.00 13.03 O HETATM 856 CB ASB A 110 10.053 14.307 8.091 1.00 11.72 C HETATM 857 CG ASB A 110 9.774 14.157 6.621 1.00 15.26 C HETATM 858 OD1 ASB A 110 10.688 14.485 5.644 1.00 19.29 O HETATM 859 OD2 ASB A 110 8.693 13.880 6.340 1.00 13.36 O HETATM 860 C1 AASB A 110 10.637 15.649 3.353 0.50 27.61 C HETATM 861 C2 AASB A 110 10.231 14.480 4.266 0.50 32.98 C HETATM 862 O1 AASB A 110 11.505 16.454 3.690 0.50 31.63 O HETATM 863 O2 AASB A 110 10.085 15.787 2.280 0.50 21.80 O HETATM 4742 O2 BASB A 110 10.072 15.815 2.191 0.50 24.78 O HETATM 4743 C1 BASB A 110 10.573 15.717 3.221 0.50 28.20 C HETATM 4744 O1 BASB A 110 11.449 16.458 3.619 0.50 22.71 O HETATM 4745 C2 BASB A 110 10.107 14.567 4.152 0.50 19.02 C HETATM 4746 F BASB A 110 9.287 13.735 3.610 0.50 34.13 F Although I have provided a new CIF file for the ligand named according to the alternate conformation this causes phenix to crash. How can I correctly refine these overlapping atoms ? Thanks for your advice, Eike

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n_gaussian tables?
by Aaron Oakley 17 Jul '18

17 Jul '18

Hi Phenixers, I gather that the wk1995 and it1992 scattering tables come from Waasmaier & Kirfe (1995), Acta Cryst. A51, 416-431 and the International Tables Vol C 1992 respectively. Can someone please tell me from where the n_gaussian scattering tables are derived? With thanks, a++

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Problems about AutoSol: too many HA sites identified.
by Kaibo Zhang 09 Jul '18

09 Jul '18

Hello, I tried to use AutoSol to solve a SAD date set. The space group is P212121, with two proteins per ASU each containing one SeMet. However, the Hyss would always find 4~5 extra sites per ASU besides the two SeMet residues. So my questions are: a. Is this normal to have so many more sites identified? Or what might be the problem? b. Could I remove those extra Se sites during refinement if the occupancy is low or doesn't make sense biologically? Here are some details: 1. Most of the extra sites are around 20% occupancy and not within the range as alternate SeMet side-chain positions. One of them even overlapped with the position where should be a ligand phosphate. 2. The 2Fo-Fc map and AutoBuild solution looked fine, but the Fo-Fc map is kinda noisy with positive peaks showing up within the main-chain density which causes troubles for refinement. 3. No twining was detected for the dataset. Several space groups have been tried (including no screw axis) and all of the solutions contained more sites than there should be. Please let me know if you encountered similar problems before. Thanks a lot! Best regards Kaibo *Kaibo Zhang* PULSe, Purdue University Hockmeyer Hall, Room 321 240 S. Martin Jischke Drive, West Lafayette, IN 47907 Telephone: 765-337-1955 E-mail: zhang644(a)purdue.edu

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Detrmining pixel size
by anaa2 08 Jul '18

08 Jul '18

Hello, Does anyone know how to accurately determine the voxel size of an EM map? If you are slightly off (i.e. 1.38 compared to 1.40 pixel) does this affect real space refinement in PHENIX? Many thanks, Noor

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Real space refinement
by Reza Khayat 08 Jul '18

08 Jul '18

Hi, What is the syntax for having phenix.real_space_refine refine a single chain of a multi-chain complex? I have separated the chains into distinct files and run refinement on a single chain (file) with undesirable results. It seems that residues adjacent to the density of a neighboring chain get pulled into the neighboring density -possibly because the neighboring density is vacant. I hope my explanation is clear. Thanks. Best wishes, Reza Reza Khayat, PhD Assistant Professor Department of Chemistry City College of New York 85 Saint Nicholas Terrace, CDI 2.318 New York, NY 10031 http://www.khayatlab.org/ 212-650-6070

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Fw: AsCA 2018/CRYSTAL 32 conference workshops
by Christopher Squire 06 Jul '18

06 Jul '18

? [https://az659834.vo.msecnd.net/eventsairseasiaprod/production-uoaevents-pub…] Dear Colleagues, Registration for the AsCA 2018/CRYSTAL 32 Conference workshops which will be held on Sunday, 2 December 2018 is now open. Delegates can register for a workshop at the same time as registering for the conference. There are four workshops which will each run concurrently. Spaces are strictly limited, so please register now at the following site: http://asca2018.org/registration/? Workshop topics: * Olex2-CCDC workshop * CCP4-Autorickshaw workshop * Combined workshop 1) SBGrid - Structural biology software infrastructure, 2) Synergistic use of diffraction and spectroscopic methods at XFEL and synchrotron sources * LCP - Lipidic cubic phase workshop For a full description of the workshops visit http://asca2018.org/workshops/ and for the full programme (including times) visit http://asca2018.org/programme/. Finally, a reminder that submissions are now open. Please visit the Call for Abstracts<http://asca2018.org/call-for-abstracts/> page for more information and to submit an abstract. Should you have any queries regarding the AsCA 2018/CRYSTAL 32 Conference, please do not hesitate to contact us using the email address below. Kind regards, Event Services University of Auckland Email: asca2018(a)auckland.ac.nz<mailto:[email protected]> [https://az659834.vo.msecnd.net/eventsairseasiaprod/production-uoaevents-pub…] ________________________________ To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1

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high level python API
by wtempel 06 Jul '18

06 Jul '18

Hi, I would like to call programs like phenix.refine from a python script. Is the python subprocess module my best bet? Or does phenix provide its own interface similar to, say, ccp4 dispatchers? Thanks. Wolfram Tempel

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Re: [phenixbb] [cctbxbb] Deprecating legacy support (CentOS 5, Windows 32-bit) in CCTBX and Phenix
by Billy Poon 06 Jul '18

06 Jul '18

Hi Luc, No worries, let us know of any other concerns. Thanks! -- Billy K. Poon Research Scientist, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory 1 Cyclotron Road, M/S 33R0345 Berkeley, CA 94720 Tel: (510) 486-5709 Fax: (510) 486-5909 Web: https://phenix-online.org On Fri, Jul 6, 2018 at 2:22 AM Luc Bourhis <luc_j_bourhis(a)mac.com> wrote: > Hi Billy, > > > Or do you need something sooner? > > No, considering the timeframe for the move to conda is before the end of > the year. I just wanted to know so that I can start advertising the change > to the people on my side. Sorry if I missed that point during the meeting > you invited me on. > > Best wishes, > > Luc > > > _______________________________________________ > cctbxbb mailing list > cctbxbb(a)phenix-online.org > http://phenix-online.org/mailman/listinfo/cctbxbb >

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Invitation to International conference "BIOMEMBRANES 2018"
by Marin, Egor 06 Jul '18

06 Jul '18

Fellow structural biologists, we are pleased to invite you to participate in the 4th biannual international C*onference* “BIOMEMBRANES 2018”, which will be held on October 1-5, 2018 at the Moscow Institute of Physics and Technology, Dolgoprudny, Moscow region, Russia. This is the first meeting within the International Conference Series “Virtual Human – Imaging Across Scales” co-organized by scientists from Russia, Germany, China, and USA. Our speakers will focus on cutting-edge problems of modern integrative structural biology of biomembranes and membrane proteins, theoretical biophysics of membrane systems and computer modelling. The conference will highlight the role of biomembranes in aging and age-related diseases such as cancer, neurodegenerative (Alzheimer’s, Parkinson’s) and cardiovascular diseases. The talks will be given by world-leading scientists from Russia, USA, Germany, France, the Netherlands, China, Spain, Italy, Sweden and Switzerland. Preliminary scientific program, as well as the up-to-date list of speakers please find here: https://biomembranes2018.ru/program/ In parallel, an international *School* “Mechanisms of aging and age-related diseases” will take place as a satellite event of the Conference on September 30 - October 5, 2018. The full information about the school will soon be available on our web-site https://biomembranes2018.ru/sa tellite-events. Early bird registration until 31.07, registration until 14.09. Further information is available on the conference web site http://biomembranes2018.ru. We are looking forward to meet you in Dolgoprudny! sincerely yours, Organizing Committee

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Re: [phenixbb] [cctbxbb] Deprecating legacy support (CentOS 5, Windows 32-bit) in CCTBX and Phenix
by Billy Poon 06 Jul '18

06 Jul '18

Hi Luc, With the planned migration to conda for dependencies, the idea is to build one linux installer using the compilers in conda (currently GCC 7.2, https://conda.io/docs/user-guide/tasks/build-packages/compiler-tools.html) and then test that installer on multiple distributions of linux. CentOS 7 would be one of the distributions used for testing. Or do you need something sooner? We currently do not build our installers on CentOS 7, but I have checked that the CentOS 6 installer runs and that the regression tests (phenix_regression.test_all_parallel, which is a superset of cctbx regression tests) pass on CentOS 7. -- Billy K. Poon Research Scientist, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory 1 Cyclotron Road, M/S 33R0345 Berkeley, CA 94720 Tel: (510) 486-5709 Fax: (510) 486-5909 Web: https://phenix-online.org On Wed, Jul 4, 2018 at 7:31 AM Luc Bourhis <luc_j_bourhis(a)mac.com> wrote: > Hi Billy, > > > The upcoming Phenix 1.14 official release will still have installers for > CentOS 5 and Windows 32-bit, but since CentOS is no longer supporting > CentOS 5, and RedHat is only supporting RHEL5 through their Extended Life > Cycle Support Add-On (until November 30, 2020), we are planning on > deprecating CentOS 5 support (32-bit and 64-bit). In addition, we are > planning on deprecating 32-bit support for Windows because only a few > percent (< 5% for both Windows and CentOS 5) of our Phenix downloads are > for 32-bit versions. > > > If you deprecate CentOS 5, will you start to support CentOS 7? I mean > right now, nightly tests run CentOS 5 & 6. Do you plan to make it 6 & 7? I > am asking so that I can start planning for Bruker among other things… > > Best wishes, > > Luc > > > _______________________________________________ > cctbxbb mailing list > cctbxbb(a)phenix-online.org > http://phenix-online.org/mailman/listinfo/cctbxbb >

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Deprecating legacy support (CentOS 5, Windows 32-bit) in CCTBX and Phenix
by Billy Poon 02 Jul '18

02 Jul '18

Hi everyone, The upcoming Phenix 1.14 official release will still have installers for CentOS 5 and Windows 32-bit, but since CentOS is no longer supporting CentOS 5, and RedHat is only supporting RHEL5 through their Extended Life Cycle Support Add-On (until November 30, 2020), we are planning on deprecating CentOS 5 support (32-bit and 64-bit). In addition, we are planning on deprecating 32-bit support for Windows because only a few percent (< 5% for both Windows and CentOS 5) of our Phenix downloads are for 32-bit versions. Please let us know if support for CentOS 5 (32-bit and/or 64-bit) or 32-bit Windows is a requirement for your systems. If so, also please describe your setup. Thanks! -- Billy K. Poon Research Scientist, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory 1 Cyclotron Road, M/S 33R0345 Berkeley, CA 94720 Tel: (510) 486-5709 Fax: (510) 486-5909 Web: https://phenix-online.org

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Incorrect secondary structure assignment in a .pdb
by Maciej Jagielnicki 29 Jun '18

29 Jun '18

Hi All, I used a combination of phenix real space refine and Coot to build a model into a cryoEM density map. I used an existing .pdb file as a starting point for my building. During the build, some helical elements became strands and vice versa (it was very clear to my eyes). Unfortunately, neither Phenix nor Coot would automatically update the header information for secondary structure elements, and I had to manually edit the header so that helices would show up in correct places when the .pdb file was viewed in Chimera or similar software. Not an ideal way of doing this which is likely related to what happened next. When the header information is removed, however, as it happens when the pdb.extract tool prepares a .pdb file for submission by turning it into a .cif file, the secondary structure elements are still displayed when a .cif file is visualized (bizzare in itself) but also the secondary structure is taken straight from the starting .pdb file (the one I used as a base for my model to which there is no connection whatsoever). The question is this - where does the incorrect secondary information come from in the absence of the header? How to fix this? I cannot deposit a file that shows helices/sheets wherever it wants... Regards, Maciej J. -- Maciej Jagielnicki, MS. Graduate Student University of Virginia Molecular Physiology and Biological Physics 480 Ray C Hunt Drive Rm 320 Charlottesville, VA Lab Phone: 434-243-2520

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Call for targets (not-yet-released structures) for CASP13 modelling experiment
by Randy Read 28 Jun '18

28 Jun '18

Posted on behalf of the CASP organizing committee: **** NB: There are only two weeks left to collect new targets for CASP13, so your contributions would be very gratefully received! **** Request for protein structures to test modeling methods - CASP13 CASP community experiments aim to establish and advance the state of the art in protein structure modeling. To this end, CASP collects information on soon-to-be released experimental structures for a three month season every two years. Sequences and other information on these targets is distributed to the protein modeling community, and the resulting models assessed by independent experts in the field. Results are published in special issues of the journal PROTEINS (see all about CASP12 at https://onlinelibrary.wiley.com/toc/10970134/86/S1). About 100 modeling groups from around the world take part. The success of CASP depends completely on the generosity of the experimental community in providing modeling targets. We are now requesting targets for the CASP13 experiment, which will launch at the beginning of May. So, if you have anything suitable, we would be most grateful if you would go to the target entry page: http://www.predictioncenter.org/casp13/targets_submission.cgi The CASP community needs modeling targets over a wide range of difficulty, for modeling with and without the aid of templates. We are particularly interested in membrane proteins, protein complexes, and cryo-EM structures. We are also extending CASP to include more modeling assisted by sparse experimental data, in collaboration with experimental groups in NMR, SAXS, chemical crosslinking, and FRET. For that, protein material is needed (of course this is not expected for most targets, but if its available, it would be much appreciated!). For those of you who have not provided targets to CASP before, the procedure is simple – there is a web page for submitting targets, and an experienced staff to deal with any queries. We don’t need the structure in advance of its release by the PDB, and if we are notified early enough (a minimum of three weeks before release, more is better) there need be no delay in structure release. More details are available on the web site. Thanks, CASP organizing committee: John Moult, University of Maryland, USA Krzysztof Fidelis, University of California, Davis, USA Andriy Kryshtafovych, University of California, Davis, USA Torsten Schwede, University of Basel, Switzerland ------ Randy J. Read Department of Haematology, University of Cambridge Cambridge Institute for Medical Research Tel: + 44 1223 336500 Wellcome Trust/MRC Building Fax: + 44 1223 336827 Hills Road E-mail: rjr27(a)cam.ac.uk Cambridge CB2 0XY, U.K. www-structmed.cimr.cam.ac.uk

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validating ~100 structures
by CPMAS Chen 26 Jun '18

26 Jun '18

Hi, All, I have about 100 structures needs be validated and optimized. what will be a fast way to do so? Can I somehow put phenix.molprobity in a circle? Thanks! -- *************************************************** Charles Chen Research Instructor University of Pittsburgh School of Medicine Department of Anesthesiology ******************************************************

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phenix.real_space_refine - Removing rotamer restraints on a per residue basis
by Ashley Pike 25 Jun '18

25 Jun '18

Hi, Is it possible to exclude particular residues from the effects of global restraints in phenix.real_space_refine? In my case rotamer restraints mucks up the sidechain fit to density for certain Phe and Tyr?. Thanks, Ashley

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Software Engineer position to work with Phaser team in Cambridge
by Randy Read 21 Jun '18

21 Jun '18

We've just advertised a position for a Software Engineer to work with us on the development of Phaser. Detailed information on the position and how to apply can be found on the University of Cambridge website (http://www.jobs.cam.ac.uk/job/17918/) and on jobs.ac.uk (http://www.jobs.ac.uk/job/BKS034/software-engineer). The text of the job description is appended, if you'd like to look at that before clicking on one of the links! Best wishes, Randy Read ================= We are looking for a graduate Software Engineer to join the group of Prof Read in the Cambridge Institute for Medical Research (http://www.cimr.cam.ac.uk/), based at the Cambridge Biomedical Campus in Cambridge. The well-established project develops mathematical methods and software for the imaging of biological molecules. The software supports academic and pharmaceutical R&D worldwide. You will be joining a small expert academic team. The successful applicant will have a careful approach to software development. Your software will be required to be reliable, algorithmically fast, and memory efficient. We have a slow development cycle and the code you write will be in use for the foreseeable future. Your individual contribution will be recognised with authorship of peer-reviewed articles; publications from our group have a track record of being highly cited. The project is funded by the National Institute of Health (USA) and the successful applicant will have the opportunity to join bi-annual collaborative meetings that cycle among Lawrence Berkeley National Laboratory (Berkeley, California), Duke University (Durham, North Carolina) and the New Mexico Consortium (Santa Fe, New Mexico). We also have an active collaboration with IBMB- CSIC (Barcelona, Spain). Software is open source (https://git.uis.cam.ac.uk/x/cimr-phaser/phaser.git/summary). We use the C++0x/C++11 standard to maintain cross-platform compilation and compatibility. You will have access to the University of Cambridge's computing resources, and a laptop will be provided. Qualifications and Experience: University degree that includes computer science and/or mathematics, experience with C++ and the Linux OS. Skills in Python scripting, GPU programming and threading would be desirable. Knowledge of biology to A level standard or equivalent would be an advantage. This appointment is full-time (37 hours/week Monday to Friday) but we welcome applications from individuals who wish to be considered for part-time working or other flexible working arrangements. Royalty payments from software will extend beyond the lifetime of the contract. University of Cambridge employment benefits include USS pension, and reduced staff fees for University of Cambridge graduate courses (see http://www.jobs.cam.ac.uk/offer/ for a full list). For more information on the research group see https://www.cimr.cam.ac.uk/research/principal-investigators/principal-inves…, and details of the Phaser project can be found at http://www.phaser.cimr.cam.ac.uk/. Fixed-term: The funds for this post are available untill 30th April 2022. ------ Randy J. Read Department of Haematology, University of Cambridge Cambridge Institute for Medical Research Tel: + 44 1223 336500 Wellcome Trust/MRC Building Fax: + 44 1223 336827 Hills Road E-mail: rjr27(a)cam.ac.uk Cambridge CB2 0XY, U.K. www-structmed.cimr.cam.ac.uk

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Postdoctoral position in membrane protein structure and function at the NIH
by Anirban Banerjee 20 Jun '18

20 Jun '18

There is an open postdoctoral position for a membrane protein structure-function project in my lab at the NIH. We are currently focusing on integral membrane enzymes (Science. 2018, doi: 10.1126/science.aao6326) and transporters of transition metal ions (J Biol Chem. 2018, doi: 10.1074/jbc.M117.817478). Here is the formal announcement - EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT, BETHESDA, MD AND SURROUNDING AREA Position Description: The research group of Dr. Anirban Banerjee at the National Institutes of Health (NIH) is seeking candidates for postdoctoral fellows . The broad interests of the lab are in membrane protein structure and function. We combine structural techniques such as macromolecular crystallography and cryo EM with biophysical and biochemical methods such as reconstitution based assays, high resolution light microscopy and small molecule screening to investigate the structural bases of the mechanisms of a number of membrane proteins. The lab has state-of-the-art equipment and facilities. We have dedicated periodic access to the 22-ID beamline at the APS, for crystallographers at the NIH, as well as access to 23-ID and 24-ID beam lines at the APS. Our laboratory is part of the Cell Biology and Neurobiology Branch in the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD). We also have an affiliation to the National Institute of Neurological Disorders and Stroke (NINDS). Qualifications: The candidates should hold a Ph. D. degree, be author of at least one first author publication and have a strong background in biochemistry or structural biology. Experience with basic molecular biology, protein expression, purification and biochemical characterization are required. Prior experience in membrane protein biochemistry or mammalian expression system for protein purification will be added advantages. It is absolutely essential the candidate is motivated and prepared to put in the best efforts for fruition of the project goals. We are a small, friendly lab and ability to work as part of a cohesive group is important. To Apply: Interested candidates can send an e-mail to anirban.banerjee(a)nih.gov with a CV and a summary of previous research experience and future interests. The NIH is dedicated to building a diverse community in its training and employment programs.

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Chair of the Department of Molecular Microbiology and Immunology at Univ. of Missouri
by Tanner, John J. 18 Jun '18

18 Jun '18

The Department of Molecular Microbiology and Immunology at the University of Missouri is searching for a new Chair. Please see the links below for information about the department and the position. I would be happy to discuss this opportunity offline with interested people. https://medicine.missouri.edu/departments/molecular-microbiology-immunology https://medicine.missouri.edu/sites/default/files/MMI_Chair_Advertisement-A… John J. Tanner Professor of Biochemistry and Chemistry Interim Chair of Biochemistry University of Missouri-Columbia 117 Schweitzer Hall Columbia, MO 65211 Phone: 573-884-1280 Fax: 573-882-5635 Email: tannerjj(a)missouri.edu<mailto:[email protected]> http://faculty.missouri.edu/~tannerjj/tannergroup/tanner.html Lab: Schlundt Annex rooms 3,6,9, 203B, 203C Office: Schlundt Annex 203A

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Table 1 successor in 3D?
by Gerard Bricogne 13 Jun '18

13 Jun '18

Dear phenixbb subscribers, I sent the message below to the CCP4BB and phenixbb at the same time last Friday. It went straight through to the CCP4BB subscribers but was caught by the phenixbb Mailman because its size exceeded 40K. Nigel, as moderator of this list, did his best to rescue it, but all his attempts failed. He therefore asked me to resubmit it, now that he has increased the upper size limit. Apologies to those of you who are also CCP4BB subscribers, who will already have received this message and the follow-up discussion it has given rise to. With best wishes, Gerard. ----- Forwarded message from Gerard Bricogne <gb10> ----- Date: Fri, 1 Jun 2018 17:30:48 +0100 From: Gerard Bricogne <gb10> Subject: Table 1 successor in 3D? To: CCP4BB(a)JISCMAIL.AC.UK, phenixbb(a)phenix-online.org Dear all, Bernhard Rupp has just published a "Perspective" article in Structure, accessible in electronic form at https://www.cell.com/structure/fulltext/S0969-2126(18)30138-2 in which part of his general argument revolves around an example (given as Figure 1) that he produced by means of the STARANISO server at http://staraniso.globalphasing.org/ . The complete results of his submission to the server have been saved and may be accessed at http://staraniso.globalphasing.org/Gallery/Perspective01.html and it is to these results that I would like to add some annotations and comments. To help with this, I invite the reader to connect to this URL, type "+" a couple of times to make the dots bigger, and press/toggle "h" whenever detailed information on the display, or selection of some elements, or the thresholds used for colour coding the displays, needs to be consulted. The main comment is that the WebGL interactive 3D display does give information that makes visible characteristics that could hardly be inferred from the very condensed information given in Table 1, and the annotations will be in the form of a walk through the main elements of this display. For instance the left-most graphical object (a static view of which is attached as "Redundancy.png") shows the 3D distribution of the redundancy (or multiplicity) of measurements. The view chosen for the attached picture shows a strong non-uniformity in this redundancy, with the region dominated by cyan/magenta/white having about twice the redundancy (in the 6/7/8 range) of that which prevails in the region dominated by green/yellow (in the 3/5 range). Clear concentric gashes in both regions, with decreased redundancy, show the effects of the inter-module gaps on the Pilatus 2M detector of the MASSIF-1 beamline. The blue spherical cap along the a* axis corresponds to HKLs for which no measurement is available: it is clearly created by the detector being too far from the crystal. The second (central) graphical object, of which a view is given in Figure 1 of Bernhard's article and another in the attached picture "Local_I_over_sigI.png") shows vividly the blue cap of measurements that were missed but would probably have been significant (had they been measured) cutting into the green region, where the local average of I/sig(I) ranges between 16 and 29! If the detector had been placed closer, significant data extending to perhaps 3.0A resolution would arguably have been measured from this sample. The right-most graphical object (of which a static view is attached as "Debye-Waller.png") depicts the distribution of the anisotropic Debye-Waller factor (an anisotropic generalisation of the Wilson B) of the dataset, giving yet another visual hint that good data were truncated by the edges of a detector placed too far. Apologies for such a long "STARANISO 101" tutorial but Bernhard's invitation to lift our eyes from the terse numbers in Table 1 towards 3D illustrations of data quality criteria was irresistible ;-) . His viewpoint also agrees with one of the main purposes of our STARANISO developments (beyond the analysis and remediation of anisotropy, about which one can - and probably will - argue endlessly) namely contribute to facilitating a more direct and vivid perception by users of the quality of their data (or lack of it) and to nurturing evidence-based motivation to make whatever extra effort it takes to improve that quality. In this case, the undeniable evidence of non-uniformity of redundancy and of a detector placed too far would give immediate practical guidance towards doing a better experiment, while statistics in Table 1 for the same dataset would probably not ... . Thank you Bernhard! With best wishes, Gerard, for and on behalf of the STARANISO developers ----- End forwarded message -----

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Coupling ligand occupancy with helix displacement
by John Michael Bruning 11 Jun '18

11 Jun '18

Hi, I have a very flexible covalent adduct that adopts three alternative conformations (A,B,C) in my structure . Conformations A and C are solvent exposed, while conformation B is buried. The buried conformation B displaces a regulatory helix (resseq 589:598) by a few angstrom, while the solvent exposed conformations do not displace this helix. I can't seem to write a occupancy .params file that fulfills: 1.) occ. of ligand conformation B = occ. of displaced helix conformation # coupling of ligand binding with helix displacement 2.) occ. non-displaced helix conformation = (1 - occ. displaced helix conformation) 3.) sum occ. ligand conformations A+B+C = 1 # assuming protein was initially labeled 100% It seems like #7 from http://www.phenix-online.org/newsletter/CCN_2015_07.pdf#page=12 is my situation, but I can't quite seem to modify this for my case. For example, something like: constrained_group { selection = chain A and resname CPE and altid B or chain A and resseq 589:598 and altid B} Captures the concerted conformation aspect (1) (occupancy for ligand conformation B = occupancy for displaced helix) and the sum occupancy of the displaced and non-displaced helix = 1 (2), but the sum of the the alternative conformations A+B+C > 1.0 (w/ A+C = 1.0) (3) Incidentally, my resolution is 2.4 Ang. Thanks for any help! Cheers, John Cheers, John *********************************** John Bruning, Post-Doctoral Scholar Stanford University, Glenn Lab CCSR Building, #3110 ***********************************

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CSHL X-ray Methods in Structural Biology Course Oct 15-30th 2018: Application deadline June 15th
by Paul Adams 05 Jun '18

05 Jun '18

Dear Colleagues, The June 15th deadline for applications to the CSHL X-ray Methods in Structural Biology Course to be held later this year, October 15 through October 30 2018, is rapidly approaching. This is a unique opportunity to become expert in the use of X-ray crystallography to solve challenging macromolecular structures. The official course announcement can be found here: https://meetings.cshl.edu/courses.aspx?course=C-CRYS&year=18 please pass this on to people who might be interested and who would benefit, including your students and postdocs. This comprehensive course is an outstanding place to learn both the theoretical and practical aspects of macromolecular crystallography, and consists of extensive lectures and practical sessions from experts in the field. The instructor team is: Alex McPherson, Bill Furey, Jim Pflugrath, Tassos Perrakis, and myself. We are assisted by world recognized experts in crystallization, data collection, data processing, structure solution, refinement, and validation (see the course link above for more details). The goal of the course is for researchers who have had some exposure to X-ray crystallography to become experts. This is an experience in macromolecular crystallography learning that cannot be found anywhere else, and the student/teacher ratio is often 1:1. We expect participants to crystallize one or more proteins and determine their structures in a two week period. Students may also work on their own projects, but not exclusively. They will become very well-versed in the theory of X-ray diffraction and crystal structure determination, while also having lots of fun. Both synchrotron data collection and in-house diffraction data collection will be used to solve structures. The course is limited to 16 participants due to the very hands-on nature of the experiments and the intimate seminar and laboratory settings. Please check the above web link for more details. In particular, please note the information about the various fellowships, scholarships, and stipends that are available. The course is supported with funds provided by the National Institute of General Medical Sciences, for which we are extremely grateful. Also there are stipends available from the Leona M. and Harry B. Helmsley Charitable Trust and the Howard Hughes Medical Institute to help offset the cost of tuition. If anyone has any questions, please send me an e-mail, we will be happy to answer all queries. Cheers, Paul -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley Lab Division Deputy for Biosciences, Advanced Light Source, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Laboratory Research Manager, ENIGMA Science Focus Area Building 33, Room 347 Building 978, Room 4126 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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Fwd: phenixbb post from [email protected]
by Nigel Moriarty 04 Jun '18

04 Jun '18

Folks There was a post from Gerard Bricogne that was lost (as far as I can see) in the internals of MailMan because of a 40Kb size limit and other reasons unknown. It was posted to the CCP4BB so you may have already seen it. Please find it below. Cheers Nigel --- Nigel W. Moriarty Building 33R0349, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory Berkeley, CA 94720-8235 Phone : 510-486-5709 Email : NWMoriarty(a)LBL.gov Fax : 510-486-5909 Web : CCI.LBL.gov Subject: Table 1 successor in 3D? Dear all, Bernhard Rupp has just published a "Perspective" article in Structure, accessible in electronic form at https://www.cell.com/structure/fulltext/S0969-2126(18)30138-2 in which part of his general argument revolves around an example (given as Figure 1) that he produced by means of the STARANISO server at http://staraniso.globalphasing.org/ . The complete results of his submission to the server have been saved and may be accessed at http://staraniso.globalphasing.org/Gallery/Perspective01.html and it is to these results that I would like to add some annotations and comments. To help with this, I invite the reader to connect to this URL, type "+" a couple of times to make the dots bigger, and press/toggle "h" whenever detailed information on the display, or selection of some elements, or the thresholds used for colour coding the displays, needs to be consulted. The main comment is that the WebGL interactive 3D display does give information that makes visible characteristics that could hardly be inferred from the very condensed information given in Table 1, and the annotations will be in the form of a walk through the main elements of this display. For instance the left-most graphical object (a static view of which is attached as "Redundancy.png") shows the 3D distribution of the redundancy (or multiplicity) of measurements. The view chosen for the attached picture shows a strong non-uniformity in this redundancy, with the region dominated by cyan/magenta/white having about twice the redundancy (in the 6/7/8 range) of that which prevails in the region dominated by green/yellow (in the 3/5 range). Clear concentric gashes in both regions, with decreased redundancy, show the effects of the inter-module gaps on the Pilatus 2M detector of the MASSIF-1 beamline. The blue spherical cap along the a* axis corresponds to HKLs for which no measurement is available: it is clearly created by the detector being too far from the crystal. The second (central) graphical object, of which a view is given in Figure 1 of Bernhard's article and another in the attached picture "Local_I_over_sigI.png") shows vividly the blue cap of measurements that were missed but would probably have been significant (had they been measured) cutting into the green region, where the local average of I/sig(I) ranges between 16 and 29! If the detector had been placed closer, significant data extending to perhaps 3.0A resolution would arguably have been measured from this sample. The right-most graphical object (of which a static view is attached as "Debye-Waller.png") depicts the distribution of the anisotropic Debye-Waller factor (an anisotropic generalisation of the Wilson B) of the dataset, giving yet another visual hint that good data were truncated by the edges of a detector placed too far. Apologies for such a long "STARANISO 101" tutorial but Bernhard's invitation to lift our eyes from the terse numbers in Table 1 towards 3D illustrations of data quality criteria was irresistible ;-) . His viewpoint also agrees with one of the main purposes of our STARANISO developments (beyond the analysis and remediation of anisotropy, about which one can - and probably will - argue endlessly) namely contribute to facilitating a more direct and vivid perception by users of the quality of their data (or lack of it) and to nurturing evidence-based motivation to make whatever extra effort it takes to improve that quality. In this case, the undeniable evidence of non-uniformity of redundancy and of a detector placed too far would give immediate practical guidance towards doing a better experiment, while statistics in Table 1 for the same dataset would probably not ... . Thank you Bernhard! With best wishes, Gerard, for and on behalf of the STARANISO developers

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d99 beyond Nyquist?
by Ricardo Righetto 03 Jun '18

03 Jun '18

Hi, I've seen the d99 criterion in phenix.mtriage reporting a resolution value beyond Nyquist (=2.0 A), or very close to Nyquist in another case. For these particular maps, which are from the same dataset processed with two different single-particle analysis packages (internal benchmarking), half-map FSC-based methods (including blocres) report resolutions in the range of 3.0-3.5 A which are consistent with the features I can see. How can I interpret this? I understand that d99 starts omitting Fourier samples from the corners of the reciprocal box, but does it make sense to report a value beyond Nyquist? I tried supplying unfiltered, masked and unmasked versions of the maps with barely any variation in the d99 results. Thanks in advance for helping figuring this out! Best wishes, -- Ricardo Diogo Righetto

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Computational Crystallography Newsletter (CCN) submissions
by Nigel Moriarty 01 Jun '18

01 Jun '18

Folks Calling for articles and short communications of interest to structural biologists. The initial deadline for submission for the July 2018 issue is 22 June 2018. The Computational Crystallography Newsletter (CCN) is an electronic newsletter for structural biologists, and is published online every 6 months. Feature articles, meeting announcements and reports can be submitted to me at any time for consideration. Submission of text by email or word-processing files using the CCN templates is requested. Past newsletters and a Microsoft Word template are available at www.phenix-online.org/newsletter. Cheers Nigel --- Nigel W. Moriarty Building 33R0349, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory Berkeley, CA 94720-8235 Phone : 510-486-5709 Email : NWMoriarty(a)LBL.gov Fax : 510-486-5909 Web : CCI.LBL.gov

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Table 1 successor in 3D?
by Gerard Bricogne 01 Jun '18

01 Jun '18

Dear all, Bernhard Rupp has just published a "Perspective" article in Structure, accessible in electronic form at https://www.cell.com/structure/fulltext/S0969-2126(18)30138-2 in which part of his general argument revolves around an example (given as Figure 1) that he produced by means of the STARANISO server at http://staraniso.globalphasing.org/ . The complete results of his submission to the server have been saved and may be accessed at http://staraniso.globalphasing.org/Gallery/Perspective01.html and it is to these results that I would like to add some annotations and comments. To help with this, I invite the reader to connect to this URL, type "+" a couple of times to make the dots bigger, and press/toggle "h" whenever detailed information on the display, or selection of some elements, or the thresholds used for colour coding the displays, needs to be consulted. The main comment is that the WebGL interactive 3D display does give information that makes visible characteristics that could hardly be inferred from the very condensed information given in Table 1, and the annotations will be in the form of a walk through the main elements of this display. For instance the left-most graphical object (a static view of which is attached as "Redundancy.png") shows the 3D distribution of the redundancy (or multiplicity) of measurements. The view chosen for the attached picture shows a strong non-uniformity in this redundancy, with the region dominated by cyan/magenta/white having about twice the redundancy (in the 6/7/8 range) of that which prevails in the region dominated by green/yellow (in the 3/5 range). Clear concentric gashes in both regions, with decreased redundancy, show the effects of the inter-module gaps on the Pilatus 2M detector of the MASSIF-1 beamline. The blue spherical cap along the a* axis corresponds to HKLs for which no measurement is available: it is clearly created by the detector being too far from the crystal. The second (central) graphical object, of which a view is given in Figure 1 of Bernhard's article and another in the attached picture "Local_I_over_sigI.png") shows vividly the blue cap of measurements that were missed but would probably have been significant (had they been measured) cutting into the green region, where the local average of I/sig(I) ranges between 16 and 29! If the detector had been placed closer, significant data extending to perhaps 3.0A resolution would arguably have been measured from this sample. The right-most graphical object (of which a static view is attached as "Debye-Waller.png") depicts the distribution of the anisotropic Debye-Waller factor (an anisotropic generalisation of the Wilson B) of the dataset, giving yet another visual hint that good data were truncated by the edges of a detector placed too far. Apologies for such a long "STARANISO 101" tutorial but Bernhard's invitation to lift our eyes from the terse numbers in Table 1 towards 3D illustrations of data quality criteria was irresistible ;-) . His viewpoint also agrees with one of the main purposes of our STARANISO developments (beyond the analysis and remediation of anisotropy, about which one can - and probably will - argue endlessly) namely contribute to facilitating a more direct and vivid perception by users of the quality of their data (or lack of it) and to nurturing evidence-based motivation to make whatever extra effort it takes to improve that quality. In this case, the undeniable evidence of non-uniformity of redundancy and of a detector placed too far would give immediate practical guidance towards doing a better experiment, while statistics in Table 1 for the same dataset would probably not ... . Thank you Bernhard! With best wishes, Gerard, for and on behalf of the STARANISO developers

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Anisotropy with TLS
by Eugene Osipov 31 May '18

31 May '18

Hi, everyone, Can someone shed a light on B-factor refinement in PHENIX.refine. I am refining the structure with 2.5 A resolution, with individual B-factors and automatically defined TLS groups. Despite isotropic refinement of B-factors I still see ANISOU entries for atoms. I figured out that these ANISOU lines appear only after TLS refinement. So the question is how these ANISOU values are calculated? -- Eugene Osipov Junior Research Scientist Laboratory of Enzyme Engineering A.N. Bach Institute of Biochemistry Russian Academy of Sciences Leninsky pr. 33, 119071 Moscow, Russia e-mail: e.m.osipov(a)gmail.com

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Berkeley Server Downtown (5/29 - 5/31)
by Billy Poon 30 May '18

30 May '18

Dear all, On Tuesday, May 29, our servers will be shut down starting at 5:00 pm Pacific for scheduled maintenance in our building. We expect that the servers will be available by 10:00 am Pacific on Thursday (5/31) at the latest. This will affect, - The Phenix web site (http://phenix-online.org/) - The DIALS West web site (http://dials.lbl.gov/) - The CCI web site (http://cci.lbl.gov/) - The Structural Biology Technology Portal (http://technology.sbkb.org/) Bug reports and emails requesting help should be queued and we will receive them once the servers are back online. We apologize for any inconvenience. -- Billy K. Poon Research Scientist, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory 1 Cyclotron Road, M/S 33R0345 Berkeley, CA 94720 Tel: (510) 486-5709 Fax: (510) 486-5909 Web: https://phenix-online.org

1 1

postdoc crystallographer job offer; International Institute in Warsaw, 15th Jun
by Błażej Bagiński 30 May '18

30 May '18

Dear All, Bujnicki Lab (Laboratory if Bioinformatics and Protein Engineering, located in the International Institute of Molecular and Cell Biology in Warsaw) is looking for an experienced (post-doc level) crystallographer/structural biologist, with an interest in combining various experimental and computational methods for structure determination of RNAs and RNA-protein complexes. Our group is involved in theoretical and experimental research on nucleic acids and proteins. The current focus is on RNA sequence-structure-function relationships (in particular 3D modeling), RNA-protein complexes, and enzymes acting on RNA. The Institute have in-house crystallographic and computing facilities and is located in the Ochota campus, surrounded by Polish Academy of Science's institutes and University of Warsaw's departments of biology/chemistry/physics/medicine/mathematics interests. Please find the full job offer in the attachment, as well as in the link below. The deadline is on 15th of June 2018. http://genesilico.pl/employment/#5 The webpage of our group can be found here; http://genesilico.pl/ as well as more information about the Institute: https://www.iimcb.gov.pl/en/ For more information and questions, please contact this address: Bujnicki, Janusz: iamb(a)genesilico.pl Kind regards, Błażej Bagiński

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d99 resolution measure availability?
by Oliver Clarke 27 May '18

27 May '18

Hi, I think the “d99” criterion described in this preprint (https://www.biorxiv.org/content/early/2018/03/14/279844) looks like a really interesting FSC-independent way to measure res in real space, and I’d like to give it a go on my maps (particularly those where I am suspicious of the FSC-based res based on map appearance, or where I suspect overfitting). Is it available in any phenix package at present? The scripts site mentioned in the preprint (http://phenix-online.org/phenix_data/afonine/cryoem_validation/) is currently rather sparsely populated. (Also, I wonder whether a directional version of the d99 criterion might be useful to estimate anisotropic res in the case of a preferred orientation, analogous to the 3D-FSC approach of Yong-Zi Tan and Dmitry Lyumkis?) Cheers Oli

4 4

rosetta refinement
by Sebastiano Pasqualato 24 May '18

24 May '18

Hi all, it seems that rosetta refinement uses test_flag_value=1 as default. Is there a way to change this? Couldn’t find it in the gui… Thanks s -- Sebastiano Pasqualato, PhD Crystallography Unit Department of Experimental Oncology European Institute of Oncology IFOM-IEO Campus via Adamello, 16 20139 - Milano Italy tel +39 02 9437 5167 fax +39 02 9437 5990

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Phenix comes with dials?
by Murpholino Peligro 17 May '18

17 May '18

[murph@localhost ~]$ dials.version DIALS 1.9.3-gb491019a-release Installed in: /home/murph/Bins/dials_stuff/dials-v1-9-3/modules/dials [murph@localhost ~]$ dials.version_1.13-2998 DIALS 1.8.0-gf5b6132-release Installed in: /home/murph/Bins/phenix_stuff/phenix-1.13-2998/modules/dials Why I never saw this on the documentation?

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Protein Crystallography Facility Manager, MRC Laboratory of Molecular Biology, Cambridge, UK
by David Barford 15 May '18

15 May '18

Dear colleagues, Please see below an advert for the position of Protein Crystallography Facility Manager at the MRC Laboratory of Molecular Biology. Protein Crystallography Facility Manager, MRC Laboratory of Molecular Biology, Cambridge, UK The MRC Laboratory of Molecular Biology (LMB) seeks to appoint a Protein Crystallography Facility Manager. The LMB is one of the birthplaces of structural biology and remains at the forefront of methods development as protein crystallography is a critical technique for understanding the mechanisms of macromolecular complexes, one of the major goals of the LMB. The post-holder will provide support to researchers from all Divisions of the LMB in the collection of X-ray diffraction data using both synchrotrons and in-house X-ray facilities, will maintain and develop the in-house facilities, will provide expert advice and support during subsequent structure determinations, and will act as the coordinator for LMB's synchrotron access. It is expected that there will be the opportunity for collaboration on structural projects with research groups at the LMB. The successful applicant will have several years of post-doctoral experience in the field of protein crystallography including data collection at synchrotrons and all aspects of structure determination. Excellent communication and inter-personal skills are required because the post will involve interacting with a diverse range of scientists with different levels of expertise. Closing date for applications: 11th June 2018 For further details and information on how to apply please visit: https://mrc.tal.net/vx/appcentre-ext/candidate/post/1707/en-GB <https://mrc.tal.net/vx/appcentre-ext/candidate/post/1707/en-GB> Informal enquires should be addressed to Dr. David Barford. E.mail: dbarford(a)mrc-lmb.cam.ac.uk <mailto:[email protected]> Dr. Jan Löwe. E.mail: jyl(a)mrc-lmb.cam.ac.uk <mailto:[email protected]> _______________________________ Dr. David Barford Structural Studies Division MRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH, UK. e.mail: dbarford(a)mrc-lmb.cam.ac.uk Tel. +44 (0)1223 267075

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Released: Phenix/DivCon Plugin - DivCon Discovery Suite v7.5.0
by Lance Westerhoff 10 May '18

10 May '18

Hello All- Some of you may have already seen this release, but I wanted to pass it along to the community as well. Today, we release version 7.5.0 of our flagship product: the DivCon Discovery Suite. This release includes fundamental improvements and a complete re-write of several key technologies leading to improved usability and a 14+ fold speedup to our Phenix/DivCon and XModeScore Crystallographic module for protomer/tautomer determination, fragment binding mode determination, and automated QM/MM X-ray refinement (including MOE-independent versions of each of those users who do not have MOE available). This version also includes a completely new tool for crystallographic "water picking" using 3DRISM. For a detailed breakdown of the new features (along with links to tutorials and other documentation), please see the following link: http://www.quantumbioinc.com/news/show/DivCon-7.5.0 As with prior releases, the software available for free for true non-profit/academic research. And of course it is available for industry use for a reasonable license fee. The list of available licenses (for electronic signature) is available here: http://www.quantumbioinc.com/products/software_licensing Thank you for your time and have a great rest of your spring! -Lance ____________________ Lance M. Westerhoff, Ph.D. President and General Manager QuantumBio Inc. WWW: http://www.quantumbioinc.com Email: lance(a)quantumbioinc.com Phone: 814-235-6908 Fax: 814-235-6909 This message and any attachments are solely for the intended recipient and should be considered confidential. If you are not the intended recipient, please immediately and permanently delete.

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European Crystallography Meeting Oviedo; Neutron Macromolecular Crystallography Satellite Meeting
by John R Helliwell 09 May '18

09 May '18

Dear Colleagues, We draw your attention to the following meeting in Oviedo, Spain in August:- https://ecm31.ecanews.org/en/neutron-macromolecular-crystallography.php Best wishes, John and Matthew Emeritus Professor John R Helliwell DSc; Dr Matthew Blakeley, Institut Laue Langevin.

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Phenix.rosetta build Ubuntu 16.04
by Joseph Brock 08 May '18

08 May '18

Dear phenix community, I am trying to get phenix to run with rosetta on my Ubuntu 16.04 station. I am running the latest official phenix version (phenix-1.13-2998) and and compiled rosetta 3.7 (2016.32.58837) using scons as described: https://www.phenix-online.org/documentation/reference/rosetta_install.html https://www.rosettacommons.org/docs/latest/build_documentation/Build-Docume… Then ran rosetta.build_phenix_interface. All went without error but running rosetta.run_tests then gave the segmentation fault below. Defining variables as suggested did not help. I found a similar question in the phenixbb archives but no resolution: http://www.phenix-online.org/pipermail/phenixbb/2013-October/020274.html Any suggestions on how to move forward greatly appreciated! Cheers, Joseph. _________________________________________________________________________________________________________ Segmentation fault (Python and libc call stacks above) This crash may be due to a problem in any imported Python module, including modules which are not part of the cctbx project. To disable the traps leading to this message, define these environment variables (e.g. assign the value 1): BOOST_ADAPTBX_FPE_DEFAULT BOOST_ADAPTBX_SIGNALS_DEFAULT This will NOT solve the problem, just mask it, but may allow you to proceed in case it is not critical. Traceback (most recent call last): File "/usr/local/phenix-1.13-2998/build/../modules/phenix/phenix/command_line/rosetta_refine.py", line 305, in <module> run(sys.argv[1:], create_dir=True) File "/usr/local/phenix-1.13-2998/build/../modules/phenix/phenix/command_line/rosetta_refine.py", line 191, in run debug=params.output.debug) File "/usr/local/phenix-1.13-2998/modules/phenix/phenix/rosetta/refine.py", line 313, in __init__ self.run_jobs() File "/usr/local/phenix-1.13-2998/modules/phenix/phenix/rosetta/refine.py", line 388, in run_jobs check_result(result) File "/usr/local/phenix-1.13-2998/modules/phenix/phenix/rosetta/refine.py", line 379, in check_result raise RuntimeError("Aborted due to error in job %d." % result.job_id) RuntimeError: Aborted due to error in job 1. Joseph S. Brock | PhD Researcher Drew Lab Department of Biochemistry and Biophysics Stockholm University

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phenix server down?
by Murpholino Peligro 02 May '18

02 May '18

Is the phenix server down? I cannot access the following links http://www.phenix-online.org/documentation https://www.phenix-online.org/download/phenix/release/ :(

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Introducing ISOLDE
by Tristan Croll 01 May '18

01 May '18

Dear members of the structural biology community, It is with great pleasure that I announce the release of version 1.0b1 of ISOLDE, a new, free for academic/nonprofit use, environment for interactive rebuilding of macromolecular models against low-medium resolution experimental crystallographic or cryo-EM maps. A paper describing ISOLDE is online at http://scripts.iucr.org/cgi-bin/paper?S2059798318002425, and you can also get an overview from my demonstration video at https://www.youtube.com/watch?v=limaUsNAVL8. In brief, though, ISOLDE is designed to help overcome the substantial challenge involved in building high-quality models into “difficult” maps (e.g. those with worse than 3Å resolution) by re imagining the task as one akin to interacting with a real, “living” molecule. At its heart is the use of interactive molecular dynamics: all atoms feel van der Waals and electrostatic interactions with their neighbours as you interact with them, avoiding clashes and constantly settling towards their nearest low-energy state. In addition to this, ISOLDE helps interpret what you're looking at by performing real-time rotamer, Ramachandran and peptide plane validation, flagging up potential problems directly on the model to give you instant feedback on the results of your actions. Specific features: - support for protein, nucleic acid, water and some small molecules/ions (with substantially expanded support to come in later versions) - start an interactive simulation covering anything from a few residues to your entire model (depending on your hardware) at the click of a button - “always-on” validation updates every time coordinates change (results are shown directly as markup on the model itself, and also accessible via more traditional tables/plots) - Interactively apply peptide plane or cis/trans flips and add/remove position, distance, rotamer and secondary structure restraints via a simple graphical interface - Smoothly shift any continuous stretch of backbone forward/backward along the chain to easily recover from register shift errors - Save a checkpoint in a running simulation and return to it with a button click, allowing you to experiment with tricky regions without fear - Real-time visualisation of crystal symmetry contacts: when the master atoms move, they move. - One-button masking of maps to cover any arbitrary atom selection – particularly useful for diagnosing large-scale problems. - Extensive GUI and API documentation, available by clicking the “Help” button in the ISOLDE GUI window. ISOLDE is built as a plugin to UCSF ChimeraX (http://preview.cgl.ucsf.edu/chimerax/download.html) and is currently available for modern Linux distros and MacOS, and can be installed from within ChimeraX via its ToolShed (Tools/More Tools...). It should run on any Linux version that supports ChimeraX itself. NOTE: due to some recent changes in the ChimeraX API, the current build will only work with the ChimeraX 0.6 release (not the version 0.7 daily builds). In terms of hardware, ISOLDE is designed based on the understanding that not everybody has access to high-performance computing facilities, so its minimum requirements are as modest as possible. The most important requirement is a GPU capable of OpenCL 1.2 or CUDA processing. My “go-to” machine for performance testing is a 2016-model gaming laptop equipped with a Nvidia GTX 1070 GPU – this achieves ~20 coordinate updates and >30 graphics updates per second with live validation on the included 229-residue demo model, indistinguishable from (or slightly faster than) my Xeon workstation. At the other end of the scale, it runs at usable speeds on my MacBook Air for simulations of a few dozen residues, sufficient for many tasks. I hope you find it useful, and enjoy using it as much as I've enjoyed making it. The MolProbity score to beat on the demo model is 1.02 (after refinement in your favourite package – ID is in the PDB header so you can download reflections from the wwPDB), and bonus points if you can identify the mystery ligand (I can't). If you recognise it as your model I apologise – I picked it out at random, I swear! Best regards, Tristan

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DNA pucker
by Dyda 30 Apr '18

30 Apr '18

Hi, Is it possible and if so how to change the pucker restraint for a particular DNA nucleotide from C2'-endo to C3'-endo in phenix.refine? I have a problem with a terminal nucleotide that is in an active site and the current C2'-endo doesn't seem consistent with the 2Fo-Fc map. Thanks for your help. [32m******************************************************************************* Fred Dyda, Ph.D. Phone:301-402-4496 Laboratory of Molecular Biology Fax: 301-496-0201 DHHS/NIH/NIDDK e-mail:[email protected] Bldg. 5. Room 303 Bethesda, MD 20892-0560 URGENT message e-mail: 2022476710(a)mms.att.net Google maps coords: 39.000597, -77.102102 http://www2.niddk.nih.gov/NIDDKLabs/IntramuralFaculty/DydaFred *******************************************************************************[m

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Abstract deadline is TOMORROW for Diffraction Methods in Structural Biology GRS
by Pearce, N.M. (Nick) 27 Apr '18

27 Apr '18

Dear BB, Tomorrow is the abstract deadline for the Gordon Research Seminar in Diffraction Methods 2018 at Bates College, Maine (28-29th July 2018). Applications/abstracts received after this date (28th April) will still be able to attend and present posters, but will not be considered for oral presentations. This year’s title is Crystallography 2.0: Restructuring the Field Around a New Wave of Experiments We want to have as many young scientists (Post-docs, PhD candidates & Master’s students) at the GRS (and associated GRC) as possible. For Jessica and myself, the 2016 Diffraction Methods GRS & GRC was the best conference we’ve attended during our PhDs, since it allowed us to present our research directly to our peers in a relaxed setting; it also gave many of us the opportunity to gain first-hand experience as session chairs -- an opportunity that is difficult to find as a young scientist. On top of this, the intimate nature and relatively small size of Gordon conferences helped us to build more long-lasting international connections than at any other conference we have attended. Of course, the GRS can only be truly successful if a wide variety of viewpoints are represented — so please consider attending. We would greatly appreciate it if you could also forward this invitation to any young scientists for whom you think this conference might be valuable. You can apply for the seminar (GRS) here: https://www.grc.org/diffraction-methods-in-structural-biology-grs-conferenc…. On this page you can also find a link to the associated Gordon Research Conference (GRC). We hope to see you in July, Nicholas Pearce & Jessica Besaw Chair & Co-Chair, Gordon Research Seminar in Diffraction Methods, 2018

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11th CCP4/APS Crystallographic School in the US
by Qingping Xu 26 Apr '18

26 Apr '18

Just a friendly reminder that the deadline for applying the upcoming CCP4 school at APS is next Wednesday (5/2/2018), please apply or finish your application (if you have already applied) if you wish to participate in the school. Please let us know if you have any questions/concerns. Qingping Xu GMCA/APS Argonne National Laboratory =========== Dear Colleagues, We are pleased to announce the *11th annual CCP4 crystallographic school *“From data collection to structure refinement and beyond” will be held on June 18-25, 2018 at Advanced Photon Source (APS), Argonne National Laboratory (ANL), near Chicago, Illinois, USA. All details can be found at http://www.ccp4.ac.uk/schools/APS-2018/index.php. *Dates*: June 18 through 25, 2018 *Location*: Advanced Photon Source, Argonne National Laboratory, Argonne (Near Chicago), Illinois, USA The school comprises two parts: *data collection workshop* and *crystallographic computing workshop*. Data collection workshop includes beamline training, data collection on GM/CA@APS beamlines 23ID-D and 23ID-B equipped with Pilatus3 6M and Eiger 16M detectors respectively, and data processing. For data collection, only the participants' crystals will be used. Crystallographic computation workshop will feature many modern crystallographic software packages taught by authors and other experts. The daily schedule will be organized in three sections – lectures, tutorials, and hands-on (interactive trouble-shooting of the technical difficulties the participants face in their projects). We have had considerable success resolving these problems in past years, attested by resulting publications (see http://www.ccp4.ac.uk/schools/APS-school/publications.php). *Applicants*: Graduate students, postdoctoral researchers and young scientists at the assistant professor level, along with commercial/industrial researchers are encouraged to apply. Only 20 applicants will be selected for participation. Participants of the workshop are strongly encouraged to bring their own problem data sets or crystals so the problems can be addressed during data collection and/or computation workshops. *Application*: Application deadline is *Wednesday May 2nd, 2018*. The application form, the program, contact info and other details can be found at http://www.ccp4.ac.uk/schools/APS-2018/index.php *Registration fees*: The registration for application is free but there is $500 participation fee for the selected academic students and $950 for the industrial researchers. The link for the on-line payments and instructions will be provided once the selection process is completed. The students will be responsible for their transportation and lodging. The workshop organizers can assist in making the lodging reservations at the Argonne Guest House. The workshop will cover all other expenses (including meals). We hope to see you at the school. Charles, Garib and Qingping

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BCA/CCP4 Summer School in Protein Crystallography at Diamond
by Airlie McCoy 23 Apr '18

23 Apr '18

Applications are now open for the BCA/CCP4 Summer School in Protein Crystallography to be held at Diamond (UK) from Monday 27th August to Saturday 1st September 2018. Note that applications close 18TH MAY 2018 The BCA/CCP4 Protein Crystallography Summer School is intended for students and researchers new to crystallography. Its dual aims are to provide comprehensive training in crystallography and to promote best practise within the British crystallographic community. The lectures cover the gamut of techniques required for a structure solution, from protein expression through to structure validation. Intensively supervised computer tutorials enable students to relate the theory presented in the lectures to practice. Although CCP4 programs will primarily be used in these tutorials, the aim will be to approach crystallographic questions in a software-agnostic manner. There will also be a crystal manipulation and cooling workshop. Note that the course is scheduled during Diamond synchrotron downtime, so there will not be active data collection at the Diamond beamlines. Up to 10 places for those with BBSRC studentships will be fully funded. We recognise that the social programme plays a role in enabling students to make links that may be maintained throughout a research career. There will be a conference dinner, and a number of other events, including a trip to Oxford. For more information see http://www.diamond.ac.uk/Home/Events/2018/BCA-Summer-School.html Application form: https://extranet2.diamond.ac.uk/ISV/BCA/ApplicationForm.aspx

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Abstract deadline is 28th April for Diffraction Methods in Structural Biology GRS
by Pearce, N.M. (Nick) 23 Apr '18

23 Apr '18

Dear BB, There are five more days until the abstract deadline for the Gordon Research Seminar in Diffraction Methods 2018 at Bates College, Maine (28-29th July 2018). Applications/abstracts received after this date (28th April) will still be able to attend and present posters, but will not be considered for oral presentations. This year’s title is Crystallography 2.0: Restructuring the Field Around a New Wave of Experiments We want to have as many young scientists (Post-docs, PhD candidates & Master’s students) at the GRS (and associated GRC) as possible. For Jessica and myself, the 2016 Diffraction Methods GRS & GRC was the best conference we’ve attended during our PhDs, since it allowed us to present our research directly to our peers in a relaxed setting; it also gave many of us the opportunity to gain first-hand experience as session chairs -- an opportunity that is difficult to find as a young scientist. On top of this, the intimate nature and relatively small size of Gordon conferences helped us to build more long-lasting international connections than at any other conference we have attended. Of course, the GRS can only be truly successful if a wide variety of viewpoints are represented — so please consider attending. We would greatly appreciate it if you could also forward this invitation to any young scientists for whom you think this conference might be valuable. You can apply for the seminar (GRS) here: https://www.grc.org/diffraction-methods-in-structural-biology-grs-conferenc…. On this page you can also find a link to the associated Gordon Research Conference (GRC). We hope to see you in July, Nicholas Pearce & Jessica Besaw Chair & Co-Chair, Gordon Research Seminar in Diffraction Methods, 2018

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mtriage error
by Sara Weaver 20 Apr '18

20 Apr '18

Hi all, I'm trying to process some cryoEM data that goes to 2.9 angstroms in phenix. I can't seem to run mtriage on several different builds. Any ideas? I've put the errors below. I've tried making my input map a .mrc, or a .ccp4 and get the same errors. Thanks! Sara [sjweaver@brmaster job099]$ /hotdata/sbgrid/programs/x86_64-linux/phenix/1.12-2829/phenix-1.12-2829/build/bin/phenix.mtriage map_file_name=run_class001.mrc ------------------------------------------------------------------------------- phenix.mtriage: Given map file and optionally model and half-map files compute map statistics. How to run: phenix.mtriage model_file_name=m.pdb map_file_name=m.map half_map_file_name_1=m1.map half_map_file_name_2=m2.map Optional: model_file_name=, half_map_file_name_1=, half_map_file_name_2= Feedback: PAfonine(a)lbl.gov phenixbb(a)phenix-online.org ------------------------------------------------------------------------------- ------------------------------------------------------------------------------- Input model: ************ No model specified. ------------------------------------------------------------------------------- Box (unit cell) info: ********************* Unit cell: (255.948, 255.948, 255.948, 90, 90, 90) Space group: P 1 (No. 1) Traceback (most recent call last): File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.12-2829/phenix-1.12-2829/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 277, in <module> run(args=sys.argv[1:]) File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.12-2829/phenix-1.12-2829/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 190, in run task_obj.run() File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.12-2829/phenix-1.12-2829/modules/cctbx_project/mmtbx/maps/mtriage.py", line 174, in run self._shift_origin() File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.12-2829/phenix-1.12-2829/modules/cctbx_project/mmtbx/maps/mtriage.py", line 204, in _shift_origin crystal_symmetry = self.crystal_symmetry) File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.12-2829/phenix-1.12-2829/modules/cctbx_project/cctbx/maptbx/__init__.py", line 112, in shift_origin_if_needed assert [sites_cart, crystal_symmetry].count(None) in [0, 2] AssertionError [sjweaver@brmaster job099]$ /hotdata/sbgrid/programs/x86_64-linux/phenix/1.13-2998/phenix-1.13-2998/build/bin/phenix.mtriage map_file_name=run_class001.mrc ------------------------------------------------------------------------------- phenix.mtriage: Given map file and optionally model and half-map files compute map statistics. How to run: phenix.mtriage model_file_name=m.pdb map_file_name=m.map half_map_file_name_1=m1.map half_map_file_name_2=m2.map Optional: model_file_name=, half_map_file_name_1=, half_map_file_name_2= Feedback: PAfonine(a)lbl.gov phenixbb(a)phenix-online.org ------------------------------------------------------------------------------- ------------------------------------------------------------------------------- Input model: ************ No model specified. ------------------------------------------------------------------------------- Box (unit cell) info: ********************* Unit cell: (255.948, 255.948, 255.948, 90, 90, 90) Space group: P 1 (No. 1) Traceback (most recent call last): File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.13-2998/phenix-1.13-2998/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 287, in <module> run(args=sys.argv[1:]) File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.13-2998/phenix-1.13-2998/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 195, in run task_obj.run() File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.13-2998/phenix-1.13-2998/modules/cctbx_project/mmtbx/maps/mtriage.py", line 204, in run self.call(func=self._compute_d_model_b0, prefix="Compute d_model_b0") File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.13-2998/phenix-1.13-2998/modules/cctbx_project/mmtbx/maps/mtriage.py", line 185, in call func() File "/hotdata/sbgrid/programs/x86_64-linux/phenix/1.13-2998/phenix-1.13-2998/modules/cctbx_project/mmtbx/maps/mtriage.py", line 295, in _compute_d_model_b0 map_data = self.box.map_data, AttributeError: 'NoneType' object has no attribute 'map_data' [sjweaver@brmaster job099]$ /hotdata/sbgrid/programs/x86_64-linux/phenix/dev-3063/phenix-dev-3063/build/bin/phenix.mtriage map_file_name=run_class001.mrc ------------------------------------------------------------------------------- phenix.mtriage: Given map file and optionally model and half-map files compute map statistics. How to run: phenix.mtriage model_file_name=m.pdb map_file_name=m.map half_map_file_name_1=m1.map half_map_file_name_2=m2.map Optional: model_file_name=, half_map_file_name_1=, half_map_file_name_2= Feedback: PAfonine(a)lbl.gov phenixbb(a)phenix-online.org ------------------------------------------------------------------------------- Traceback (most recent call last): File "/hotdata/sbgrid/programs/x86_64-linux/phenix/dev-3063/phenix-dev-3063/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 274, in <module> run(args=sys.argv[1:]) File "/hotdata/sbgrid/programs/x86_64-linux/phenix/dev-3063/phenix-dev-3063/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 158, in run params = inputs.params) File "/hotdata/sbgrid/programs/x86_64-linux/phenix/dev-3063/phenix-dev-3063/modules/cctbx_project/mmtbx/maps/mtriage.py", line 130, in __init__ box = self.params.use_box) File "/hotdata/sbgrid/programs/x86_64-linux/phenix/dev-3063/phenix-dev-3063/modules/cctbx_project/iotbx/map_and_model.py", line 115, in __init__ crystal_symmetry = self._model.crystal_symmetry()) AttributeError: 'NoneType' object has no attribute 'crystal_symmetry' ariel:20180417_lookingatRefinej348_focused sjweaver$ /Applications/phenix-dev-3112/build/bin/phenix.mtriage map_file_name=run_ct8_class001.mrc ------------------------------------------------------------------------------- phenix.mtriage: Given map file and optionally model and half-map files compute map statistics. How to run: phenix.mtriage model_file_name=m.pdb map_file_name=m.map half_map_file_name_1=m1.map half_map_file_name_2=m2.map Optional: model_file_name=, half_map_file_name_1=, half_map_file_name_2= Feedback: PAfonine(a)lbl.gov phenixbb(a)phenix-online.org ------------------------------------------------------------------------------- Traceback (most recent call last): File "/Applications/phenix-dev-3112/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 339, in <module> run(args=sys.argv[1:]) File "/Applications/phenix-dev-3112/build/../modules/cctbx_project/mmtbx/command_line/mtriage.py", line 204, in run inputs.model.setup_scattering_dictionaries( AttributeError: 'NoneType' object has no attribute 'setup_scattering_dictionaries' -- Sara J. Weaver *Doctoral Candidate, Jensen Lab* *California Institute of Technology*

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Protein structures sought for CASP13
by Paul Adams 20 Apr '18

20 Apr '18

Posted on behalf of the CASP organizing Committee: Critical Assessment of Techniques for Protein Structure Prediction (CASP) community experiments aim to advance the state of the art in protein structure modeling. Every other year since 1994, CASP collects information on soon-to-be released experimental structures, passes on sequence data to the structure modeling community, and collects blind predictions of structure for assessment. About 100 modeling groups from around the world participate. Results of CASP experiments are published in special issues of the journal PROTEINS (e.g., CASP12: https://onlinelibrary.wiley.com/toc/10970134/86/S1). The success of CASP depends on the generosity of the structure determination community. We are now requesting targets for CASP13 experiment, which will launch at the beginning of May. The CASP community needs modeling targets over a wide range of difficulty, for modeling with and without the aid of templates. X-ray, NMR and cryo-EM structures are welcome. We are particularly interested in membrane proteins, protein complexes, and cryo-EM structures. We are also extending CASP to include more modeling assisted by sparse experimental data, in collaboration with experimental groups in NMR, SAXS, SANS, crosslinking, and FRET. For that, protein material is needed (of course this is not expected for most targets, but if available, it would be much appreciated!). So, if you have anything suitable, we encourage you to mark your PDB deposition as a "CASP target" in the PDB's submission system. Alternatively, you can suggest your protein to CASP directly through the CASP13 target entry page: http://www.predictioncenter.org/casp13/targets_submission.cgi. For those of you who have not provided targets to CASP before, the procedure is simple and fast. We don’t need the structure in advance of its release by the PDB, and if we are notified early enough (a minimum of three weeks before release, more is better) there need be no delay in structure release. More details are available on the web site. CASP target providers are regularly invited to contribute to special issue papers, for example: 2018: Kryshtafovych A, Albrecht R, Baslé A, Bule P, Caputo AT, Carvalho AL, Chao KL, Diskin R, Fidelis K, Fontes CMGA, Fredslund F, Gilbert HJ, Goulding CW, Hartmann MD, Hayes CS, Herzberg O, Hill JC, Joachimiak A, Kohring GW, Koning RI, Lo Leggio L, Mangiagalli M, Michalska K, Moult J, Najmudin S, Nardini M, Nardone V, Ndeh D, Nguyen TH, Pintacuda G, Postel S, van Raaij MJ, Roversi P, Shimon A, Singh AK, Sundberg EJ, Tars K, Zitzmann N, Schwede T. (2018). Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016). Proteins 86 (S1), 27-50. doi: 10.1002/prot.25392. PMID: 28960539 2016:  Kryshtafovych A, Moult J, Baslé A, Burgin A, Craig TK, Edwards RA, Fass D, Hartmann MD, Korycinski M, Lewis RJ, Lorimer D, Lupas AN, Newman J, Peat TS, Piepenbrink KH, Prahlad J, van Raaij MJ, Rohwer F, Segall AM, Seguritan V, Sundberg EJ, Singh AK, Wilson MA, Schwede T. (2016). Some of the most interesting CASP11 targets through the eyes of their authors. Proteins 84 (S1), 34-50. doi: 10.1002/prot.24942. PMID: 26473983   2014: Kryshtafovych A, Moult J, Bales P, Bazan JF, Biasini M, Burgin A, Chen C, Cochran FV, Craig TK, Das R, Fass D, Garcia-Doval C, Herzberg O, Lorimer D, Luecke H, Ma X, Nelson DC, van Raaij MJ, Rohwer F, Segall A, Seguritan V, Zeth K, Schwede T. (2014). Challenging the state-of-the-art in protein structure prediction: Highlights of experimental target structures for the 10th critical assessment of techniques for protein structure prediction experiment CASP10. Proteins 82 (S2), 26-42. doi: 10.1002/prot.24489. PMID: 24318984 2011: Kryshtafovych A, Moult J, Bartual SG, Bazan JF, Berman H, Casteel DE, Christodoulou E, Everett JK, Hausmann J, Heidebrecht T, Hills T, Hui R, Hunt JF, Seetharaman J, Joachimiak A, Kennedy MA, Kim C, Lingel A, Michalska K, Montelione GT, Otero JM, Perrakis A, Pizarro JC, van Raaij MJ, Ramelot TA, Rousseau F, Tong L, Wernimont AK, Young J, Schwede T. (2011). Target highlights in CASP9: Experimental target structures for the critical assessment of techniques for protein structure prediction. Proteins 79 (S10), 6-20. doi: 10.1002/prot.23196. PMID: 22020785 Thanks, CASP organizing committee: John Moult, University of Maryland, USA Krzysztof Fidelis, University of California, Davis, USA Andriy Kryshtafovych, University of California, Davis, USA Torsten Schwede, University of Basel, Switzerland Get in touch: casp(a)predictioncenter.org More information: http://www.predictioncenter.org/casp13/index.cgi Submit a target: http://www.predictioncenter.org/casp13/targets_submission.cgi -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley Lab Division Deputy for Biosciences, Advanced Light Source, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Laboratory Research Manager, ENIGMA Science Focus Area Building 33, Room 347 Building 978, Room 4126 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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Deadline for the EM and the X-ray bundles of iNEXT extended to 24 April (midnight)
by a.perrakis＠nki.nl 19 Apr '18

19 Apr '18

Dear all, The deadline for the EM and the X-ray bundles of iNEXT is now extended until 24 April (midnight, for all timezones …). For more information http://www.inext-eu.org/inext-em-and-x-ray-bundles/ and to submit a proposal https://www.structuralbiology.eu/submit-proposal/?t=inext Best regards, the INEXT team

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