- phenixbb - phenix-online.org

Phasing@Home event
by Claudia Millán Nebot 05 Jun '20

05 Jun '20

Dear PhenixBb community, We are glad to announce the first Phasing@Home event, an online meeting devoted to presenting XDS, ARCIMBOLDO, Phaser and SHELX software and their use in challenging phasing cases. Confirmed speakers and members of the teams: Institut de Biologia Molecular de Barcelona (IBMB-CSIC): Isabel Usón, Claudia Millán, Ana Medina, Iracema Caballero, Elisabet Jimenez, Albert Castellví, Giovanna Petrillo, Josep Triviño Cambridge Institute for Medical Research (CIMR): Randy Read, Airlie McCoy, Rob Oeffner, Kaushik Hatti, Massimo Sammito, Tristan Croll University of Konstanz: Kay Diederichs University of Goettingen: George Sheldrick Instituto de Biociencias, Universidade Estadual Paulista (UNESP): Rafael Borges The full schedule can be found under: http://chango.ibmb.csic.es/phasingathome The meeting will hosted via Zoom and is free of charge but you will need to pre-register here: https://www.eventbrite.co.uk/e/phasinghome-tickets-107673520398 The event will be held online on the 13th and 14th of July. Talks will be short and focused on covering the advanced usage of the software, so participants are expected to be familiar with the basics already or to browse some basic material provided by us in advance. Interaction among speakers and participants will be through a Discord (https://discord.com/) server. Please note that this event is limited to 25 external participants and provided they meet the requirements of presenting some challenging dataset, the acceptance upon registration will be on a first-come, first-served basis. With best wishes, ---------------------------------------------------------------------------------------- Claudia Millán (cmncri(a)ibmb.csic.es) Crystallographic Methods Group http://chango.ibmb.csic.es Institut de Biologia Molecular de Barcelona (IBMB-CSIC) Barcelona, Spain LinkedIn: es.linkedin.com/in/claudiamillan/ <http://es.linkedin.com/pub/claudia-mill%C3%A1n/60/a76/821/> ResearchGate: https://www.researchgate.net/profile/Claudia_Millan?ev=hdr_xprf Twitter: https://twitter.com/cheshireminima and Massimo Sammito

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Amber module in phenix on Ubuntu 18.04
by Guenter Fritz 04 Jun '20

04 Jun '20

Dear all, dear Nigel, I cannot get the Amber and AFITT menu bars in the phenix.refine GUI on a Ubuntu (Xubuntu 18.04) box. I set Preferences "Enable alpha-test programs and features" (works on my Mac 10.14.6 and SciLinux6 box ). Moreover, on the Xubuntu machine: when I start the phenix.refine GUI (phenix version 1.18.2-3874) I see the following error message in the terminal running phenix: //$ phenix// /Could not import the compiled Python-sander interface. Make sure you have the Python development libraries installed and that you have sourced amber.sh or amber.csh / //------------------------// python 3.7 is installed and python development tools :/ / /------------------------ / /$ python -V // //Python 3.7.6 / /$ sudo apt list -a python3.7-dev // //Listing... Done // //python3.7-dev/bionic-updates,now 3.7.5-2~18.04 amd64 [installed] // //python3.7-dev/bionic-security 3.7.3-2~18.04.1 amd64 // //python3.7-dev/bionic 3.7.0~b3-1 amd64 / /------------------------/ Any idea what is going wrong? Thanks a lot and best regards, Guenter

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Post-doctoral position in Neutron/X-ray crystallography at the Institut Laue Langevin (Grenoble, FR)
by Nicolas Coquelle 03 Jun '20

03 Jun '20

Dear all, The Large Scale Structure group of the Institut Laue Langevin (Grenoble, FR), in collaboration with the group of Elspeth Garman (Oxford, UK) has an open position for a post-doctoral fellow in neutron/X-ray crystallography to study radiation-damage. Please see the description below and contact me (coquelleni(a)ill.fr <mailto:[email protected]>) for further information. Best regards, Nicolas Coquelle.

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Imposing bond restraints across the asymmetric unit
by Brandon J Anson 27 May '20

27 May '20

Hello, I have an unusual problem in which my enzyme (a dimer) is covalently bound to its own C-terminus and so is daisy-chained across the crystal lattice. In the past, I have encountered and fixed this problem by extracting the covalent part of the molecule and re-phasing using that as the molecular replacement model. In this case, I am not able to due so. When I input the restraints, it either crashes refine or attempts to impose them on the corresponding residues within the ASU (understandable) but they are quite distal and this leads to "interesting" refinement results. Is there a good way of making phenix.refine do what I want? Or perhaps a workaround that I haven't considered yet? Best Regards, Brandon

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Refinement problem in phenix
by Muhammad Bashir Khan 23 May '20

23 May '20

Hi there; I find some unknown density in my map, where I put SO4 and in some UNX. I merged and save all in one PDB. I run ReadySet to make cif. file, but refinement still not working. Can anybody explain what else I should provide? Thanks in advance Bashir -- ------------------------------------------------------ Muhammad Bashir Khan, Ph.D. Research Associate Department of Biochemistry Medical Science Bldg. Lab 3-27 University of Alberta Edmonton AB, T6G 2H7 Phone: 780-492-4577- e-mail: mbk(a)ualberta.ca <cbrooks1(a)ualberta.ca>

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symmetry conflicts
by Daniel Larsson 22 May '20

22 May '20

I want to report an annoying bug in version 1.18.2-3874. My real_space_refine job ended with an error at the validation step saying Crystal symmetry mismatch between different files. This was when refining a PDB structure (first processed using ready_set) in a cryo-EM map. The “Ignore symmetry conflicts” checkbox was checked. The expected output files were generated, but no validation report was generated. Regards, Daniel När du har kontakt med oss på Uppsala universitet med e-post så innebär det att vi behandlar dina personuppgifter. För att läsa mer om hur vi gör det kan du läsa här: http://www.uu.se/om-uu/dataskydd-personuppgifter/ E-mailing Uppsala University means that we will process your personal data. For more information on how this is performed, please read here: http://www.uu.se/en/about-uu/data-protection-policy

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byron bender
by Taufiq El-Mokdad 22 May '20

22 May '20

Hi all, I am a student from Halle in Germany. I really want to try out doing a wire model for proteins with the Byron Bending machine, yet I couldn’t find out where to get one and the Charles Supper Company discontinued selling these devices. I was recommended asking here for help. Is there anybody still having one of these devices in their labs or having one starting to rust in a box in the attic? I would be really statisfied trying out making some wire protein models with it. If someone would be willing to give such a machine and I would of course pay the shipping costs I would be happy to hear about. I would also be grateful if someone could give me a tip where I could still ask? Thanks.. All the best Taufiq

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Alternative conformation on special position occupancy wrong
by Kaiser, Jens T. 20 May '20

20 May '20

Hi, We have a case of a cofactor with 222 symmetry in two states on a special position ( 2-fold). When modelling one state, Phenix correctly restrains the occupancy to 0.5. When putting state 2 in alternative conformation group B, the occupancy of altconf A and B is restrained to 1.0, instead of 0.5; it seems like it does not recognize that the alternative conformations are on a special position. Cheers, Jens Sent from Mail<https://go.microsoft.com/fwlink/?LinkId=550986> for Windows 10

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Phenix version 1.18 released
by Paul Adams 20 May '20

20 May '20

The Phenix developers are pleased to announce that version 1.18 of Phenix is now available (build 1.18.2-3874). Binary installers for Linux, Mac OSX, and Windows platforms, and the source installer, are available at the download site: http://phenix-online.org/download/ Please note that this recent publication should now be used to cite the use of Phenix: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Liebschner D, Afonine PV, Baker ML, Bunkóczi G, Chen VB, Croll TI, Hintze B, Hung LW, Jain S, McCoy AJ, Moriarty NW, Oeffner RD, Poon BK, Prisant MG, Read RJ, Richardson JS, Richardson DC, Sammito MD, Sobolev OV, Stockwell DH, Terwilliger TC, Urzhumtsev AG, Videau LL, Williams CJ, Adams PD: Acta Cryst. (2019). D75, 861-877. https://doi.org/10.1107/S2059798319011471 Highlights for the 1.18.2 version of Phenix: 1.18.2 Changes - Fix weighting for iron sulfur clusters 1.18.1 Changes - General bug fixes 1.18 Changes - Amber - Automatic creation of Amber files in phenix.refine GUI - Added AmberPrep GUI - Restraints - Engh & Huber restraints (2001) for cis-peptides now implemented - Restraints added for FeS - Metal coordination library is default to Zn+2 and FeS clusters - Rama-Z: New global Ramachandran score for identifying protein structures with unlikely stereochemistry in CLI (phenix.rama_z, mmtbx.rama_z) and GUI (validation reports). - Density modification for cryo-EM - Includes model-based density modification with automatic model generation - Optimized defaults and additional documentation - Real-space refinement - Hydrogen atoms no longer included in map target function, which improves fit. - Add NQH flip option (enabled by default) - Other - New tool for ordered solvent picking in cryo-EM maps (phenix.douse) - New map and model superposition tool (phenix.match_maps) - New FindProgram to find any Phenix program with a text search - Project details now has a button for opening the README file for tutorials For a full list of changes see: http://www.phenix-online.org/documentation/CHANGES Please note that this new publication should be used to cite the use of Phenix: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Liebschner D, Afonine PV, Baker ML, Bunkóczi G, Chen VB, Croll TI, Hintze B, Hung LW, Jain S, McCoy AJ, Moriarty NW, Oeffner RD, Poon BK, Prisant MG, Read RJ, Richardson JS, Richardson DC, Sammito MD, Sobolev OV, Stockwell DH, Terwilliger TC, Urzhumtsev AG, Videau LL, Williams CJ, Adams PD: Acta Cryst. (2019). D75, 861-877. https://doi.org/10.1107/S2059798319011471 Full documentation is available here: http://www.phenix-online.org/documentation/ There is a Phenix bulletin board: http://www.phenix-online.org/mailman/listinfo/phenixbb/ Please consult the installer README file or online documentation for installation instructions. Direct questions and problem reports to the bulletin board or: help(a)phenix-online.org and bugs(a)phenix-online.org Commercial users interested in obtaining access to Phenix should visit the Phenix website for information about the Phenix Industrial Consortium. The development of Phenix is principally funded by the National Institute of General Medical Sciences (NIH) under grant P01-GM063210. We also acknowledge the generous support of the members of the Phenix Industrial Consortium. -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, LBL (http://biosciences.lbl.gov/divisions/mbib) Principal Investigator, Computational Crystallography Initiative, LBL (http://cci.lbl.gov) Vice President for Technology, the Joint BioEnergy Institute (http://www.jbei.org) Principal Investigator, ALS-ENABLE, Advanced Light Source (http://als-enable.lbl.gov) Division Deputy for Biosciences, Advanced Light Source (https://als.lbl.gov) Laboratory Research Manager, ENIGMA Science Focus Area (http://enigma.lbl.gov) Adjunct Professor, Department of Bioengineering, U.C. Berkeley (http://bioeng.berkeley.edu) Adjunct Professor, Comparative Biochemistry, U.C. Berkeley (http://compbiochem.berkeley.edu) Building 33, Room 250 Building 978, Room 4126 Building 977, Room 180C Tel: 1-510-486-4225 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Ashley Dawn [ ashleydawn(a)lbl.gov ][ 1-510-486-5455 ] --

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Generating a polder map using coordinates
by Petr Kolenko 20 May '20

20 May '20

Dear colleagues, Is there a way to calculate the polder map in a selected box using coordinates instead of atom selection as shown in the "Generating a polder map with the compute_box option" website? Best regards, Petr

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Solving a protein - ligand structure
by Tom Vanmarcke 20 May '20

20 May '20

Dear, We are trying to solve a protein structure that contains a ligand (polyoxometalate). We found the ligand in the electron density but through the middle of the ligand goes a 2 fold axis. For this reason, we placed the occupendency of the ligand on 0.50. When we try to refine the structure using phenix.refine, the ligand breaks down even when adding a cif restrain file. The cif restrain file contains information about atoms, angles and bond lengths. Is there a way to fix this problem? Greetings Sent from Mail<https://go.microsoft.com/fwlink/?LinkId=550986> for Windows 10

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Is there a way to evaluate batch pdb models with Malprobity in phenix?
by Jing Liu 19 May '20

19 May '20

Hi, I had generate a batch of pdb models (40-100) in rosetta and am wondering whether there is a way to evaluate these models in batch with Molprobity. For example, can I use phenix command line to do it and how? Or should I download the Molprobity and do it on my local computer? Really appreciate if anyone can share their experience. Jing Liu, PhD Ted Jardetzky lab Department of Structural Biology Stanford University

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Phenix 1.18 and rotamer outliers
by Xavier Brazzolotto 18 May '20

18 May '20

I’ve installed the latest stable Phenix version (1.18). I’ve noticed a clear difference in the final statistics (MOLprobity) compared to the previous version (1.17). A bit more of Rama outliers and the most noticeable in the Rotamer outlier score. Is there any reason that could explain such behaviour ? I am using Phenix under MacOS. Xavier Brazzolotto, PhD xavier.brazzolotto(a)chemdef.fr Département de Toxicologie et Risques Chimiques Unité Neurotoxiques Institut de Recherche Biomédicale des Armées 1 Place du Général Valérie André, BP 73 91223 Brétigny sur Orge France Phone +33 (0) 1 78 65 14 00 Alt Phone +33 (0) 4 57 42 87 19 Cell +33 (0) 6 58 36 39 09 The information in this e-mail may be privileged and confidential, intended only for the use of the addressee(s) above. Any unauthorized use or disclosure of this information is prohibited. If you have received this e-mail by mistake, please delete it and immediately contact the sender. This is not an official email address of the French Ministry of the Armed Forces. It does not allow diffusion of protected informations and does not necessarily complies to the ministry cyber security policy.

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unit cell dimesions
by Thomas, Leonard M. 13 May '20

13 May '20

Hello All, I have run into something that has me a bit puzzled. When finishing up a structure we ended reprocessing the data to get nice statistics for deposition, I don’t want to get into that discussion. Upon reprocessing the unit cell dimensions shifted slightly, 0.05 A or so. The PDB file used had the unit cell from the original solution/refinement while the data set cell dimensions were different. I ran the newly processed reflection data set through the reflection editor in order to transfer the Rfree set. Now the really odd thing is that I ended up reprocessing a couple times and transferring over the Rfree set once more. The cell dimensions on the final reflection file is from not the original reflection file/PDB but one that was used with an intermediate cutoff between the two, it is not the cell dimensions in the input reflection either. Just for completeness the data were processed using XDS at SSRL. My question is where does phenix.refine pick up the unit cell dimensions and were does the reflection file editor pick them up? Best Regards Len Leonard Thomas, Ph.D. Macromolecular Crystallography Laboratory Oklahoma COBRE in Structural Biology Price Family Foundation Institute of Structural Biology University of Oklahoma Department of Chemistry and Biochemistry Stephenson Life Sciences Research Center 101 Stephenson Parkway Norman, OK 73019-5251 Office: (405)325-1126 lmthomas(a)ou.edu<mailto:[email protected]> http://www.ou.edu/structuralbiology/cobre-core-facilities/mcl

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install fail in linux
by 안우찬 12 May '20

12 May '20

Hi, I have a problem with install phenix-1.18.1-3865 in linux. My linux version is NAME="Red Hat Enterprise Linux Atomic Host" VERSION="7.4.0.4". The error massage is ============================================================================= Traceback (most recent call last): File "./bin/install.py", line 244, in <module> installer(sys.argv[1:]).install() File "/home01/x1959a02/phenix/phenix-installer-1.18.1-3865-intel-linux-2.6-x86_64-centos6/li b/libtbx/auto_build/install_distribution.py", line 190, in install self.check_directories() File "/home01/x1959a02/phenix/phenix-installer-1.18.1-3865-intel-linux-2.6-x86_64-centos6/li b/libtbx/auto_build/install_distribution.py", line 268, in check_directories os.makedirs(i) File "/usr/lib64/python2.7/os.py", line 157, in makedirs mkdir(name, mode) ============================================================================= Thanks in advance, Teddy Ahn

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How to compare between electron density maps?
by Murpholino Peligro 12 May '20

12 May '20

I want to compare electron density features of map A from protein A and map B from protein B... Because each map has a different rmsd level... ...what is the best way to compare electron density between maps? Is there a way to normalize maps or something like that? Thanks

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Is there a way to search the phenixbb mailing list archive?
by Murpholino Peligro 11 May '20

11 May '20

With the ccp4bb at https://www.jiscmail.ac.uk/cgi-bin/webadmin I can search for a term in the archive. Is there something similar in the phenixbb? Thanks Or... is there a way to wget all the gz files?

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Online Course on Neutron Scattering Applications in Structural Biology
by Meilleur, Flora 11 May '20

11 May '20

ORNL Online Course on Neutron Scattering Applications in Structural Biology (https://conference.sns.gov/event/217/) June 1 - June 5, 2020 2:00 pm - 5:30 pm EST Registration (free) is now open and will close May 17, 2020. This online course is designed for graduate students, post-doctoral researchers and faculty with knowledge of structure and function of biological macromolecules but with limited to no experience with neutron sciences. The course will cover the basics of deuterium labeling, small angle neutron scattering, neutron reflectometry, neutron spectroscopy, neutron imaging and neutron crystallography. Instrumentation, sample preparation, data collection and processing will be introduced for each neutron technique.

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Boost 1.70 update for cctbx
by Billy Poon 09 May '20

09 May '20

Hi everyone, There is currently a pull request for cctbx that will update Boost to 1.70 ( https://github.com/cctbx/cctbx_project/pull/409). The update enables support for Python 3.7 and 3.8. The plan is to merge this next Friday, May 8, at 3 pm Pacific. After merging, developers should delete the build/lib/*boost* files and build/boost directory so that any remnants of the old Boost are removed and then rebuild. Let me know if you have any questions. 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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Phenix installation
by Sam Tang 06 May '20

06 May '20

Hi I am installing Phenix on a Fedora 30 station. It complains line 15: /usr/bin/python: No such file or directory. I have checked that there is python3.7.3 pre-loaded. So did I miss anything obvious...? Brs Sam

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Ligand refinement - geometry does not fit density
by Schulz, Eike-Christian 04 May '20

04 May '20

Dear all, I am refining a structure with a simple ligand in phenix 1.14. The ligand is present in 2 conformations at approx. equal occupancy. Refinement of the 2 conformations runs smoothly, but 2 problems occur 1. One of the ligand atoms is placed out of the electron density after refinement. The geometry file (via elbow) is present during refinement. The atom is not in an extreme position or clashes with anything else. 2. After refinement the ligand conformation cannot be changed in coot, although I import the cif dictionary. Any advise ? Best, Eike

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Phenix 1.18 RSR runtime
by Hannah Bridges 02 May '20

02 May '20

Dear Phenix developers, We have updated to phenix version 1.18-3845-000 and found that realspace refinement (5 cycles) with minimization global, local grid search and ADP is taking about 36 hours, compared to ~ 1hr in versions 1.17 and 1.16. The slow step is the local grid search which is taking >6 hours each cycle. We are very glad for the option to run the job detached, but I wondered if this sort of timing was expected for this version? Best wishes Hannah -- Dr Hannah Bridges Investigator Scientist MRC Mitochondrial Biology Unit The Keith Peters Building University of Cambridge Cambridge Biomedical Campus Hills Road Cambridge CB2 0XY United Kingdom Telephone : 01223 252812

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off-topic; suggestions for 96head liquid handler
by Georg Mlynek 30 Apr '20

30 Apr '20

Dear Scientific community, we have lend over Viaflow96 liquid handler (used for pipetting 35-50 uL in 96 well crystallization plates) to our Covid -19 Diagnostics Initiative. As we believe that this story will be ongoing for some longer time I am looking for a new 96 head liquid handler. We are happy with the Viaflow and have two heads 10-300 uL; 0.5-12.5 uL. However one tip box (96 tips for the 10-300 uL) is about 4 €. This compares to ~1 € for the refilling racks we use for our single channel pipettes (It is said that boxes have to be more rigid, because of pressure during tip loading). Therefore if you have a 96 head liquid handler for volumes of 20-60 uL where cheap tips can be used (automation not necessary) please write me. Many thanks in advance, best regards, Georg.

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Computational Crystallography Newsletter (CCN) release and submissions
by Nigel Moriarty 28 Apr '20

28 Apr '20

Folks Recent world events have affected many things including the timely release of the CCN. Please consider this the Shelter-In-Place edition. Many of you will be involved in SARS-CoV-2 research and the CCN for July 2020 can be a vehicle for publishing the more community interest details. The deadline for submissions is 1 JUN 2020. 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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Open postdoc positions in the Gonen lab
by Johan Hattne 26 Apr '20

26 Apr '20

Dear all; We would like to draw your attention to two HHMI-funded postdoc positions in the laboratory of Tamir Gonen at the University of California, Los Angeles. The first position concerns the biochemistry of membrane proteins, the second is focused on computational methods development. For further information, as well as application instructions, see the links below. Biochemistry https://hhmi-openhire.silkroad.com/epostings/index.cfm?fuseaction=app.jobin… Programming https://hhmi-openhire.silkroad.com/epostings/index.cfm?fuseaction=app.jobin… // Best wishes; Johan

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Two conformation of a ligand
by Muhammad Bashir Khan 22 Apr '20

22 Apr '20

Hi All; I have a structure where I believe that the ligand is bind in two conformations. In the Ligand Fit, it places only one even I select conformer 2. My other question is, Is there a way that I can use a reference PDB bound to the ligand in the Ligand Fit to help it placing my ligand. Thanks for your help in advance Bashir -- ------------------------------------------------------ Muhammad Bashir Khan, Ph.D. Research Associate Department of Biochemistry Medical Science Bldg. Lab 3-27 University of Alberta Edmonton AB, T6G 2H7 Phone: 780-492-4577- e-mail: mbk(a)ualberta.ca <cbrooks1(a)ualberta.ca>

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Problems displaying disulphide links
by Urvashi Sharma 21 Apr '20

21 Apr '20

Dear all, I have a problems displaying disulphide links in PyMoL and CCP4mg for a 2.3 angstrom crystal structure. I have tried both PyMoL and CCP4mg, these programs are not recognizing an important inter-domain disulphide bridge which seems to have no problems in "Coot". While other intra-domain disulphide links are fine. Can anyone suggest how to manually fix it? In addition, I have performed protein-protein docking using this crystal structure and have obtained nice convincing model. However, in this pose, which is being refined and energy minimized, none of the disulphide links are intact! Upon manual examination, I have noticed that the corresponding cysteine are 3.0-4.0 angstrom away. How should I correct this? Looking forward to your suggestions... With thanks and regards, Urvashi ---------------------------------------------------- Dr Urvashi Sharma, DBT-Ramalingaswamy faculty fellow JNU, New Delhi.

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Error log
by Viswanathan Chandrasekaran 16 Apr '20

16 Apr '20

Hi all, Other than resubmitting the job, is there a way to retrieve the contents of the Phenix error dialog box that appears at the end of a failed job? It is not present in the log file. Thanks, Vish

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iNEXT-Discovery: Access to facilities for structural biology research
by a.perrakis＠nki.nl 16 Apr '20

16 Apr '20

Dear all, While being in turbulent times, iNEXT-Discovery, the EC Horizon-2020 project offering access to facilities for structural biology (EM, NMR, X-rays and macromolecular biophysics), has officially started its operations. iNEXT-Discovery encourages applications for structural biology projects for ‘translational research projects’ in the areas of biomedicine, biotechnology, biomaterials and in the food sector, in particular from non-experts and for researchers from academia and industry. We are now happy to announce to the wider research community our new website with details about the project and where applications for access to the participating facilities can be submitted: https://inext-discovery.eu<https://inext-discovery.eu/> Regardless of current corona-measures external researchers are more than welcome to apply for access and we expect reviewing of incoming proposals to proceed as normal. However, please keep in mind that most facilities are currently not operational, and it is uncertain when they will open again to deliver access and to receive visitors. We will not be able to give a detailed overview about the status of all facilities, as the situation is changing almost daily. Having accepted applications in our access pipelines will help both our scheduling and yours. Our facilities can arrange experiments for approved user projects to be executed immediately after local policies allow. Please note that applications addressing SARS-CoV-2 or Covid-19 and mentioning this in the title will be funneled towards rapid review. Operational facilities will prioritize such projects if they can be accommodated. On behalf of the iNEXT-Discovery team, Hans Wienk (Project Manager) - email h.wienk.AT.nki.nl<http://h.wienk.at.nki.nl/> for questions about access Anastassis Perrakis (Coordinator)

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covalently linked ligand
by Muhammad Bashir Khan 15 Apr '20

15 Apr '20

Hi All; I have a protein molecule and a ligand structure. I want to make a covalent bond between the ligand and protein molecule, could somebody explain to me how I can do that using phenix. I used the " *phenix.ligand_linking pdb_file_name" commond* It creates apply_link.def and data_link.cif I did refine the structure again giving the above file as well but did not see any covalent bond created between the protein and ligand. Thanks for your help Bashir -- ------------------------------------------------------ Muhammad Bashir Khan, Ph.D. Research Associate Department of Biochemistry Medical Science Bldg. Lab 3-27 University of Alberta Edmonton AB, T6G 2H7 Phone: 780-492-4577- e-mail: mbk(a)ualberta.ca <cbrooks1(a)ualberta.ca>

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helix/sheet outliers
by Casper Larsen 14 Apr '20

14 Apr '20

Hi.. I am doing real space refinement on a protein model build from a cryo-em map. I run the refinement with Amber gradients turned on and with secondary structure restraints (otherwise, more or less default settings). I have some issues with helix and sheet outliers. Every time I run the refinement (after making sure that the bond distance in the helices are within the 3.5 Å) I get a lot of bad annotation remarks, but with outliers just above 3.5 Å (see .log below): ... removed outlier: 3.576A pdb=" N VAL A 179 " --> pdb=" O LEU A 175 " (cutoff:3.500A) Proline residue: A 180 - end of helix removed outlier: 3.681A pdb=" N PHE A 188 " --> pdb=" O LEU A 184 " (cutoff:3.500A) removed outlier: 3.628A pdb=" N PHE A 189 " --> pdb=" O ILE A 185 " (cutoff:3.500A) removed outlier: 3.521A pdb=" N ILE A 190 " --> pdb=" O ALA A 186 " (cutoff:3.500A) Processing helix chain 'A' and resid 219 through 228 removed outlier: 3.737A pdb=" N MET A 227 " --> pdb=" O GLU A 223 " (cutoff:3.500A) ... Is this something that I just need to fix in several rounds of refinement or is there an explanation? Amber gradients maybe? In addition, I have some bad sheet annotations such as: ... removed outlier: 6.987A pdb=" N VAL B 433 " --> pdb=" O LEU B 440 " (cutoff:3.500A) removed outlier: 4.659A pdb=" N VAL B 442 " --> pdb=" O LEU B 431 " (cutoff:3.500A) removed outlier: 6.296A pdb=" N LEU B 431 " --> pdb=" O VAL B 442 " (cutoff:3.500A) removed outlier: 5.062A pdb=" N ALA B 444 " --> pdb=" O THR B 429 " (cutoff:3.500A) removed outlier: 6.129A pdb=" N THR B 429 " --> pdb=" O ALA B 444 " (cutoff:3.500A) ... When I look at the model, the residues are definitely a part of the sheet - the long distance between the N-O atoms is due to the O being "flipped" (hope it makes sense). Is this because of wrong annotation? Best Casper

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Advanced Light Source open for COVID-19 related research
by Paul Adams 14 Apr '20

14 Apr '20

Dear Colleagues, A quick note to alert researchers to the status of the Advanced Light Source in Berkeley (https://als.lbl.gov): The ALS is now operating in a limited capacity supporting COVID-19 related research. A number of MX beamlines from the ALS-ENABLE program are now taking proposals from the general user community working on COVID-19 via the ALS RAPIDD program (https://als.lbl.gov/rapidd/); choose ALS-ENABLE as the beamline and your proposal will receive prompt review with fast turnaround for beamtime. We are evaluating the possibility of expanding access to include to other techniques such as soft X-ray tomography, and BioSAXS in the near future. Please feel free to contact me with any questions. Cheers, Paul -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, LBL (http://biosciences.lbl.gov/divisions/mbib) Principal Investigator, Computational Crystallography Initiative, LBL (http://cci.lbl.gov) Vice President for Technology, the Joint BioEnergy Institute (http://www.jbei.org) Principal Investigator, ALS-ENABLE, Advanced Light Source (http://als-enable.lbl.gov) Division Deputy for Biosciences, Advanced Light Source (https://als.lbl.gov) Laboratory Research Manager, ENIGMA Science Focus Area (http://enigma.lbl.gov) Adjunct Professor, Department of Bioengineering, U.C. Berkeley (http://bioeng.berkeley.edu) Adjunct Professor, Comparative Biochemistry, U.C. Berkeley (http://compbiochem.berkeley.edu) Building 33, Room 250 Building 978, Room 4126 Building 977, Room 180C Tel: 1-510-486-4225 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Ashley Dawn [ ashleydawn(a)lbl.gov ][ 1-510-486-5455 ] --

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app which can calculate the number of reflections for a given unit cell, spacegroup, resolution?
by Georg Mlynek 13 Apr '20

13 Apr '20

Dear Scientific community, I am looking for an app which can calculate the number of reflections for a given unit cell, spacegroup, resolution. Preferred would be a graphical output too. The program XRayView http://www.phillipslab.org/downloads comes very close what I imagine but it is not possible to select a spacegroup. It would like to use it for teaching parts of practical part during lockdown. Many thanks, br Georg.

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Two Ph.D. studentships at Newcastle University, UK Prof. Bert van den Berg
by Arnaud Basle 13 Apr '20

13 Apr '20

Dear All, Please see the attached documents for two Ph.D. studentships at Newcastle University, UK. The positions are in Prof. Bert van den Berg's laboratory and informal inquiries should be directed to him (Bert.Van-Den-Berg(a)newcastle.ac.uk). Cheers, Arnaud -- Dr Arnaud Basle X-ray facilities manager Newcastle Structural Biology Laboratory Biosciences Institute Faculty of Medical Sciences Newcastle University Framlington place NE2 4HH Newcastle upon tyne Phone 0191 208 5482

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Postdoctoral position in the Korostelev Lab
by Loveland, Anna 12 Apr '20

12 Apr '20

Postdoctoral position open at the University of Massachusetts Medical School, in the Korostelev Lab: https://www.umassmed.edu/korostelev-lab/. We study translation regulation, using cryo-EM and biochemistry. We are particularly interested in: (1) Translation accuracy; (2) Ribosome's central role in bacterial stress signaling and gene regulation; (3) Neurodegenerative and other diseases, which originate from dysregulation of translation. References to some lab publications are provided below. Our laboratory is housed at the RNA Therapeutics Institute, a vibrant and highly interactive research community: https://www.umassmed.edu/rti/about-the-rti/faculty-members/. Our colleagues are interested in nearly all aspects of RNA biology, from small to large RNAs to RNA chemistry and therapeutics development. We seek a highly motivated person who very recently received a PhD, or will soon receive a PhD. Applications sent prior to the dissertation defense date are welcome. Please submit the following information via email to: ann.powers(a)umassmed.edu 1) your CV (including publication list); 2) in less than 2 pages, an outline of your: (i) previous work - focusing on your most interesting finding(s); (ii) your current/future scientific interests, and whether/which aspects of translation regulation sound interesting to you; 3) email addresses of three references. Selected publications (accessible via the provided links): - Svidritskiy et al. “Extensive ribosome and RF2 rearrangements during translation termination<https://elifesciences.org/articles/46850>”. eLife.2019. - Loveland et al. “Ensemble cryo-EM elucidates the mechanism of translation fidelity<https://www.nature.com/articles/nature22397>”. Nature. 2017. - Demo et al. “Structure of RNA polymerase bound to ribosomal 30S subunit<https://elifesciences.org/articles/28560>”. eLife. 2017. - Abeyrathne et al. “Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome<https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4896748/>”. eLife. 2016. - Loveland et al. “Ribosome•RelA structures reveal the mechanism of stringent response activation<https://elifesciences.org/articles/17029>”. eLife. 2016. --- Anna Loveland, Ph.D. anna.loveland(a)umassmed.edu 617 610 4321 (cell) Confidentiality Notice: This e-mail message, including any attachments, is for the sole use of the intended recipient(s) and may contain confidential, proprietary and privileged information. Any unauthorized review, use, disclosure or distribution is prohibited. If you are not the intended recipient, please contact the sender immediately and destroy or permanently delete all copies of the original message.

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Problem with molecular replacement
by Shramana Chatterjee 09 Apr '20

09 Apr '20

Hi, I am trying to solve a structure using a data solved by SAD as an reference (ensemble in phaser). The structure I am trying to solve has 100% sequence identity with the solved one. The problem that I am facing during Phaser MR is that, in the solved structure there are 6 molecules in the ASU although I am getting maximum 4 molecules in the ASU and also Rfree is around 0.49 just after the phaser. Phaser is showing a good values of LLG (>500) and TFZ (>8). It would be very helpful if I get any suggestion about the above-mentioned problem. Thank you in advance.

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Re: [phenixbb] Problem with molecular replacement
by Shramana Chatterjee 09 Apr '20

09 Apr '20

Thanks Roger. I am trying through looking at packing of crystal lattice.It seems that there are some gaps in the lattice. May be this is identical with the solved one because of identical cell dimension and space group. Although I think I should cross check with lattice as Matthew's analysis suggest a different number of copies. On Thu, Apr 9, 2020 at 8:51 AM Roger Rowlett <rrowlett(a)colgate.edu> wrote: > For MR solutions with more than 4 molecules in the ASU, you can improve > your chances of finding a solution by employing the following > considerations: > > The number of protein units in the ASU predicted by Matthew's analysis my > not be accurate for n>4. Always look at the molecular packing of potential > solutions in the ASU using Coot or Pymol. You may discover you have too > many molecules, and therefore overlaps, or too few molecules, leaving > protein size gaps in the crystal lattice. Lattice packing of partial > solutions may guide your thinking about the correct number of molecules in > the ASU. A good solution should normally have symmetrical and clear solvent > channels, and good contacts between all molecules. > > You may nave a better chance of obtaining a initial solution by searching > with dimers (if structurally appropriate) than monomers. > > Unless your crystal form is identical to the solved version, there is no > guarantee your N will be the same as the solved N molecules in the ASU. Use > the Matthew's analysis and lattice packing as your guide. > > Using this approach I've been able to obtain MR solutions for ASUs with > N=6-8, even with identities as low as 30%. > > Good luck. > > Roger Rowlett > Gordon & Dorothy Kline Professor, Emeritus > Colgate University > > > On Wed, Apr 8, 2020, 11:43 PM Shramana Chatterjee <schatter90(a)gmail.com> > wrote: > >> Hi, >> >> I am trying to solve a structure using a data solved by SAD as an >> reference (ensemble in phaser). The structure I am trying to solve has 100% >> sequence identity with the solved one. The problem that I am facing during >> Phaser MR is that, in the solved structure there are 6 molecules in the ASU >> although I am getting maximum 4 molecules in the ASU and also Rfree is >> around 0.49 just after the phaser. Phaser is showing a good values of LLG >> (>500) and TFZ (>8). >> >> It would be very helpful if I get any suggestion about the >> above-mentioned problem. >> >> Thank you in advance. >> >> >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://phenix-online.org/mailman/listinfo/phenixbb >> Unsubscribe: phenixbb-leave(a)phenix-online.org > >

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refinement of EM models with hydrogens using phenix.real_space_refine
by Coudray, Nicolas 08 Apr '20

08 Apr '20

Hi all, We had a question regarding how the phenix.real_space_refine works when used to refine CryoEM models with hydrogens: are hydrogens treated as riding or are they explicitly refined? Regards, Nicolas

2 2

LINK to chromophore
by 김경현[ 교수 / 생명정보공학과 ] 06 Apr '20

06 Apr '20

Hi, I get linking problems of the CRF chromophore in GFP, where the peptide bonds connecting to each end of the chromophore to the protein do not show planar configuration. The LINK cif seems to only constrain bonds and angles. Any help how to fix the planar peptide bonds at the connecting ends? Many thanks. Regards, Kyung hyun == Prof. Kyung Hyun Kim, Ph.D. Rm 244 R&D Center Green Campus Korea University Anam dong, Sungbuk gu, Seoul 136-701 Department of Biotechnology & Bioinformatics Korea University Sejong Campus, Sejong, Korea Tel : +82 2 3290 3444, +82 10 9014 1416 Homepage : *sbl.korea.ac.kr <http://sbl.korea.ac.kr>*

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ISOLDE 1.0b5 release
by Tristan Croll 06 Apr '20

06 Apr '20

Hi all, For those still lucky enough to be working on molecular model building during this crisis, I've just pushed ISOLDE 1.0b5 out to the ChimeraX ToolShed (to work with the ChimeraX 0.93 release version - download from http://preview.cgl.ucsf.edu/chimerax/download.html#release, then install ISOLDE from within ChimeraX via Tools/More Tools...). While development has been a little light since version 1.0b4 due to travel in February and then, well... everything since, there are a few new features and bug-fixes worth downloading for: - Perhaps the biggest improvement isn't actually mine - thanks to some stellar work by Tom Goddard at UCSF, ChimeraX's ribbon drawing is now ten times faster than before. Particularly for those working with very large models, this drastically reduces the lag time upon finishing an interactive simulation and returning to the default display mode. - I've done some optimisations to the methods for choosing the initial map contour levels and the MDFF coupling constant (how strongly the map "pulls" on the model during simulations). They're now about 20 times faster, removing most of the delay on initial preparation of a model for ISOLDE. - If you're lucky enough to be working on a multi-GPU machine, you can now explicitly specify the GPU to use for simulations with the command "isolde set gpuDeviceIndex {a number}" (you may need to experiment to work out which GPU is which) - You can adjust the number of simulation steps between GUI updates with "isolde set timeStepsPerGuiUpdate". This is particularly useful for slower GPUs - your simulation won't actually run faster, but your experience of it will be much smoother. The default value of 50 works well for high-end GPUs; for (for example) light-weight MacBook GPUs a value of 10 may be more suitable. Performance curves for a few of the machines available to me can be found at https://isolde.cimr.cam.ac.uk/performance-benchmarks/. - The command "clipper symmetry #{model number}" will draw a unit cell with all rotational symmetry and screw axes (mirror symmetry is not yet handled). The depiction is still a work in progress, but the fundamentals are there. - While not new to 1.0b5, a reminder that since 1.0b4 ISOLDE is fully compatible with ChimeraX's session save/restore. The command "save {filename}.cxs" will save your current session (including your model(s), all custom restraints, maps, weightings and visualisation state) to a file which can be reopened on the same or another machine to pick up exactly where you left off. Known bug: (seemingly only) on Linux machines, certain links to the help files (e.g. by typing "usage isolde" on the command line and then clicking the "isolde adjust distances"link in the log) sometimes cause segmentation faults if the help browser is not already open, crashing ChimeraX. This appears to be a bug in the Qt 5.12 web browser implementation, but so far has proven near-impossible to isolate. To avoid it, simply make sure the help browser is open (Help/User Guide) before clicking any links in the log. I very much hope you find it useful. Stay healthy! Tristan

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Update on COVID-19 Open Structures initiative
by Randy Read 03 Apr '20

03 Apr '20

Dear all, Last week I posted the message below, suggesting an open science approach to ensure that there will be no unnecessary delays in the determination of crystal structures related to COVID-19, whether they’re from the SARS-CoV-2 virus, interacting host proteins, or complexes. Working together, and combining expertise in data analysis, structure determination and computational modelling, we believe we can greatly accelerate progress on difficult structures. Since last week we’ve chosen a platform, Microsoft Teams, to coordinate the effort, created a new Team and built the bare bones of a site ready for new targets. (For those who prefer other collaboration platforms such as Slack or Zulip, they might well have advantages but I had easy access to the Teams infrastructure and we’re already using it for working from home.) If you believe that you can bring expertise to this initiative and you’re willing to share your insights and any promising results immediately with others, please get in touch and I’ll add you to the team. If you have diffraction data for a target structure for this initiative, please send an email to me, to Massimo Sammito (mds83(a)cam.ac.uk) and to the CASP organisers (casp(a)predictioncenter.org). Either Massimo or I will add you to the team, upload the target data, links and other information and send an alert to everyone who has registered. Best wishes, Randy Read =========== The Covid-19 crisis is bringing out the best in the communities we belong to, with many people giving deep thought to how we can use our skills to help. On the crystallography bulletin boards we've seen offers to help in solving Covid-19-related structures that prove difficult, offers to help with improving protein stability, suggestions that the deposition of raw diffraction images would allow the community to help get the best possible version of any relevant structure, and requests to share bioinformatics analyses and predictions of what are the most interesting targets. We're writing to suggest an additional way that the community can help to accelerate progress in the structural understanding of Covid-19. The CASP (Critical Assessment of Structure Prediction) organisers have recently launched an initiative to mobilise the structure prediction community to predict and refine 3D structures of SARS-2-Covid proteins and relevant complexes that either have unknown structure or are non-trivial modelling targets: http://predictioncenter.org/caspcommons/index.cgi. Note that the models will be refined much more extensively than typically done in a normal CASP round, which should make them even better than the impressive results seen in recent years. We would like to build on this initiative, and the enthusiasm this has revealed in the prediction community, to help to accelerate the determination of structures needed for a molecular-level understanding of Covid-19. Structure prediction has reached a level of maturity where predicted ab initio models and distant homology models can be accurate enough to solve new structures by molecular replacement. The best way to bring the prediction and experimental communities together to exploit these developments and accelerate progress is to embrace an open science approach. To that end, we propose the following: * If you have diffraction data involving a SARS-2-Covid protein, a host protein relevant to pathogenesis or a complex, but you are not immediately able to solve the structure, contact the CASP organisers (casp(a)predictioncenter.org) with the sequence(s) of the construct(s) that went into the crystallisation drop. If relevant predictions have already been made, any unreleased models will be released at this point (along with predictions of local accuracy). If proteins in your crystals are not already modelling targets, the CASP organisers will consider them as potential new targets for the modelling community. * We all want the fastest possible progress on scientific understanding of Covid-19, and this can best be achieved by completely open science. On a number of occasions at crystallographic computing schools and workshops, we have seen extremely difficult structures yield to the combined expertise of a number of developers and "power users" of the software, none of whom knew how to solve every problem that arose. Even before CASP models are available, some other crystallographer may find a way to solve the structure! So it would be ideal if the sequence information you provide to the CASP organisers was accompanied by a DOI or URL pointing at the diffraction data, preferably in the form of raw images as well as integrated data. Data from different crystal forms or poorly isomorphous crystals can also be incredibly valuable. Openness should go both ways, so people who wish to access these data will be asked to agree to immediately release any positive results, even if these fall short of a full structure solution, so that others can build on them. Best wishes, Randy Read (in cooperation with the CASP organisers) ----- Randy J. Read Department of Haematology, University of Cambridge Cambridge Institute for Medical Research Tel: +44 1223 336500 The Keith Peters 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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<no subject>
by Werther, Rachel A 02 Apr '20

02 Apr '20

Dear All, My colleague and I are troubleshooting a Phaser run that her Phenix was not able to solve but mine was. We both use the Graphical User Interface, and we both use the current version, Phenix 1.17.3644 Her log file shows “ELLG TARGET 120” and “RFACTOR CUTOFF 35.00”. If these settings are the reason one run gave the right solution and the other didn’t, how do we access and change these settings? I attached both the log files. Right.log gave the right solution, Wrong.log gave the wrong solution. Many thanks, Rachel Werther Rachel Werther / Research Technician III / Stoddard Lab / Basic Sciences / Fred Hutchinson Cancer Research Center / rwerther(a)fredhutch.org<mailto:[email protected]> / 206-667-4066

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COVID-19 protease inhibitors - 2nd call for designs - Thurs midnight
by Frank von Delft 01 Apr '20

01 Apr '20

All - last week's call for compound designs to the CoV-2 main protease (https://covid.postera.ai/covid) elicited an astonishing response... (I confess I was quite taken aback.) I just realised I should let this BB know the second call for designs is now open. *Deadline is tomorrow 23:59 PST (April 2nd). *(Apologies for those that weren't following on twitter.)* *Two things: * we're asking for designs especially focusing on covalent inhibitors (read more here <https://discuss.postera.ai/t/screening-cascade-fast-track-and-regular-track…>) * the most convincing designs will be fast-tracked by spending more money to cut several weeks off the testing (read more here <https://discuss.postera.ai/t/screening-cascade-fast-track-and-regular-track…>) Happy designing! Frank

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Postdoc position, Sugar Transporting Membrane Proteins (Denmark), repost
by Bjørn Panyella Pedersen 30 Mar '20

30 Mar '20

Dear colleagues, Repost of our postdoc position. Deadline is in 3 days. Please pass this along any one who might be interested. Thanks! /Bjørn Postdoctoral position in Structure of Sugar Transporting Membrane Proteins at Aarhus University, Denmark. online posting: http://tiny.cc/MBG_postdoc We are looking for a highly skilled and motivated postdoc with an interest in working on sugar transporting membrane transporters and preferably with a proven track record in the area of structural and/or functional analysis of membrane proteins. The position will be open from summer 2020, but starting date is negotiable. Funding is available for at least 2 years of employment, with an automatic extension possible for up to a total maximum of 4 years. The position: The position seeks to strengthen ongoing activities in the laboratory of Bjørn P. Pedersen on structure, related to the function and mechanism of sugar-transporting membrane proteins (pedersenlab.dk). The laboratory's interest is the interplay between structure and function of transmembrane transport processes with a focus on metabolite uptake systems, and the methods uses are primarily crystallography, cryo-EM and biochemistry. The group is part of the Section of Structural Biology at Aarhus University. The candidate: A successful candidate has a relevant Ph.D. degree and a solid and documented background in structural biology, biochemistry and/or biophysics. Experience with membrane protein expression and purification is favored, and the candidate must demonstrate an ability and interest to work with membrane proteins with a structural aim. Applicants should be ambitious, show strong collaborative skills, and be able to take initiatives and responsibility within the work environment. The successful candidate is offered: - access to a well-developed research infrastructure. - a research climate inviting lively, open and critical discussion within and across different fields of research. - a working environment with teamwork, close working relations, network activities among young scientists and social activities. - a workplace characterized by professionalism, equality and a healthy work-life balance. The city: In Aarhus you have easy access to beautiful nature, an exciting culture and city life as well as a safe environment for children - a great place for the whole family. The city of Aarhus has everything you need: exciting national and international jobs, delightful residential areas, a rich cultural life, and beautiful surrounding landscape of woods and coastline that make Aarhus a wonderful place to live and work. Deadline: All applications must be made online (http://tiny.cc/MBG_postdoc) and received by 2. apr. 2020.

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insert ligand restraints in real space refinement
by Valerie Biou 27 Mar '20

27 Mar '20

Hello I am trying to impose restraints on my lipid ligand during real space refinement. I found the command refinement.geometry_restraints.edits.scale_restraints { atom_selection = "resname LLP" scale = 2.5 apply_to = *bond *angle dihedral chirality I have 2 questions 1) can those lines be called from the GUI and where? if not, how can I insert them in a previous command file? 2) what do the * stand for? is it to activate or cancel the selection of an item? sorry if those questions have been asked before, I can't find the command to browse the bb archive. All the best, Valérie

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Raw diffraction images for SARS-CoV-2 related structures
by Gerard Bricogne 27 Mar '20

27 Mar '20

Dear all, It is a pleasure to be able to end the (GMT) week by calling for a huge round of applause for the Diamond team, who this afternoon started uploading a large collection of sets of raw diffraction images (77 as we write but the upload is still ongoing) for PDB entries that were released two days ago. Special thanks to Graeme Winter who organised the upload to Zenodo. The datasets are collectively accessible via the following link: https://zenodo.org/search?page=1&size=20&q=keywords:%22SARS-CoV-2%20main%20… Graeme asked that "major kudos [be given] to Zenodo developers who have been very responsive with helping us do automated downloads". Happy scrutiny and reprocessing of these datasets, and re-refinement of the associated structures, to all hard-core MX addicts! With best wishes, Clemens & Gerard. -- On Thu, Mar 19, 2020 at 10:00:11AM +0000, John Berrisford wrote: > Dear all > > The wwPDB OneDep system allows depositors to provide DOIs of raw > diffraction images during deposition to the PDB and once again > encourages depositors to provide a DOI for raw images when they have > submitted. > > Out of the 9665 X-ray entries that were released in 2019 we have DOI's > for raw images in 205 of these entries. > > We would encourage depositors to provide the DOI for their raw images > when they are available. > > Regards > > John > > > On Mar 19 2020, at 9:48 am, Joel Sussman <joel.sussman(a)WEIZMANN.AC.IL> wrote: > > > 19-Mar-2020 > > Dear Loes, Peter, Clemens & Gerard, > > I concur that it is crucial to preserve the original diffraction data > > and make it available to anyone who would like to use it. > > As an example, please see the very recent paper by > > Nachon et al (2020). "A second look at the crystal structures of > > Drosophila melanogaster acetylcholinesterase in complex with tacrine > > derivatives provides Insights concerning catalytic intermediates and > > the design of specific insecticides" Molecules 25 pii: E1198 > > [https://www.ncbi.nlm.nih.gov/pubmed/32155891]. > > The study reexamines the original data, with modern software tools, > > the original data of a paper we published in 2000 (~20 years ago) and > > revealed features that had not been noticed. Specifically > > 1) previously unmodeled density in the native active site can be > > interpreted as stable acetylation of the catalytic serine. > > 2) Similarly, a strong density in the DmAChE/ZA complex, originally > > attributed to a sulfate ion, is better interpreted as a small molecule > > that is covalently bound. The complex is reminiscent of the > > carboxylate/BChE complexes observed in crystal structures of hBChE > > [Brazzolotto et al, 2012; Nicolet et al, 2003], and demonstrates the > > remarkable ability of ChEs to stabilize covalent complexes with carboxylates. > > Thus, the study demonstrates that updated processing of older > > diffraction images, and the re-refinement of older diffraction data, > > can produce valuable information that could not be detected in the > > original analysis, and strongly supports the preservation of the > > diffraction images in public data banks. > > Best regards > > Joel > > ------------------------------------------------------------------------------------ > > Prof. Joel L. Sussman. Joel.Sussman(a)weizmann.ac.il www.weizmann.ac.il/~joel > > Dept. of Structural Biology tel: +972 (8) 934 6309 proteopedia.org > > Weizmann Institute of Science fax: +972 (8) 934 6312 > > Rehovot 76100 ISRAEL mob: +972 (50) 510 9600 > > ------------------------------------------------------------------------------------- > > > > > >> On 19 Mar 2020, at 11:32, Kroon-Batenburg, L.M.J. (Loes) > >> <l.m.j.kroon-batenburg(a)UU.NL> wrote: > >> > >> Dear Gerard, > >> > >> This is a great idea. Of course I am very much in favour of making > >> available raw diffraction images, and such a virtual workshop could > >> demonstrate the usefulness of reprocessing raw diffraction data and > >> structural refinements. I am not at all afraid that archiving of raw > >> data that are the basis of a scientific paper will have significant > >> environmental effects: this is minor compared to our everyday use of > >> cloud services. And as Graeme mentioned: when archiving raw data > >> make sure to add sufficient and correct meta data. > >> > >> Best wishes, > >> Loes > >> > >> ___________________________________________________________ > >> Dr. Loes Kroon-Batenburg > >> Dept. of Crystal and Structural Chemistry > >> Bijvoet Center for Biomolecular Research > >> Utrecht University > >> Padualaan 8, 3584 CH Utrecht > >> The Netherlands > >> > >> E-mail : l.m.j.kroon-batenburg(a)uu.nl > >> phone : +31-30-2532865 > >> fax : +31-30-2533940 > >> > >> Van: CCP4 bulletin board <CCP4BB(a)JISCMAIL.AC.UK> namens Gerard > >> Bricogne <gb10(a)GLOBALPHASING.COM> > >> Verzonden: woensdag 18 maart 2020 23:30 > >> Aan: CCP4BB(a)JISCMAIL.AC.UK <CCP4BB(a)JISCMAIL.AC.UK> > >> Onderwerp: [ccp4bb] Raw diffraction images for SARS-CoV-2 related structures > >> > >> Dear colleagues, > >> > >> Perusal and some initial (re-)refinement of the various SARS-CoV-2 protease > >> structures in the PDB seems to indicate that that there might be potential > >> to improve these if refinements could be repeated after some reprocessing > >> and further analysis of the raw diffraction images, rather than > >> against the > >> deposited merged data. This statement should in no way be construed > >> as a > >> criticism of the remarkable achievements of the research groups concerned, > >> who have been operating under tremendous time pressure, but as an exciting > >> opportunity to push methods to their limits on a uniquely significant class > >> of structures. > >> > >> Another consideration is that the various logistical problems created by > >> COVID-19 may soon make it increasingly difficult to collect new diffraction > >> data on potential drug targets relevant to the fight against SARS-CoV-2, > >> underlining the importance of ensuring that the best results be obtained > >> from every dataset actually collected, and that the most useful conclusions > >> be drawn from the analysis of those datasets towards improving the quality > >> of subsequent data collections. > >> > >> On this basis we would like to propose that special efforts be made > >> to grant > >> public access to the raw image data associated with any SARS-CoV-2 related > >> structure that is deposited into the PDB. This can be done by (1) archiving > >> these raw image data using resources such as data.sbgrid.org, zenodo.org, > >> proteindiffraction.org or any other cloud-based data-sharing service, and > >> (2) communicating the corresponding DOIs to the wwPDB centres. This idea > >> could be extended to datasets that investigators would like to offer to > >> interested methods developers or expert users at the pre-deposition stage. > >> > >> Experts making use of those raw data would be encouraged to document, > >> in as > >> much detail as possible, how particular programs or workflows could > >> be used > >> on those structures/datasets to obtain the best results. This would > >> be a > >> kind of "virtual workshop", a particularly valuable collective > >> activity at > >> the present time when several in-person workshops (e.g. RapiData) > >> have been > >> cancelled and many meetings are in limbo for several months. > >> > >> The latter activity would benefit from having a centralised facility > >> set up > >> for the experts to post their results and annotations: we could > >> create such > >> a facility, but other, larger groups might want to consider doing so. > >> > >> > >> With best wishes, > >> > >> Clemens & Gerard. > >> > >> ######################################################################## > >> > >> To unsubscribe from the CCP4BB list, click the following link: > >> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 > >> > >> To unsubscribe from the CCP4BB list, click the following link: > >> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 > > > > > > To unsubscribe from the CCP4BB list, click the following link: > > https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 > > ######################################################################## > > 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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Public resource for the structures, validation and re-modelling of Corona virus macromolecules
by Andrea Thorn 27 Mar '20

27 Mar '20

Dear colleagues, we are methods developers in structural biology. During this time of crisis, we decided to put our brains to where our hearts are and have started a public resource for the structures from beta-coronavirus with a focus on SARS-CoV and SARS-CoV-2: https://github.com/thorn-lab/coronavirus_structural_task_force It can be used to download all relevant structures, look at structural validation information, diagnostic data for the quality of experimental data and available re-refinements. We will expand this resource in time, but as of today, it contains all deposited SARS-CoV and SARS-CoV-2 structures, sorted by protein and virus, PDB-REDO entries, diffraction data diagnostics from AUSPEX and PHENIX.XTRIAGE, WHATCHECK reports and Tristan Croll's fantastic manual ISOLDE re-refinements. We will soon add MOLPROBITY to lighten the traffic on the server at Duke, individual links to Global Phasing's efforts in re-processing and re-refinement of individual structures and HARUSPEX map annotations for the Cryo-EM structures. We may point out potential improvements in some structures in these data, but this is not meant as criticism of the achievements of the researchers who first elucidated these structures! It merely reflects on recent progress in methods development and the potential to push our methods to their limit in order to get every last bit of biological information from a given data set. We hope this can make a (small) difference for a cure of COVID-19. If you have any questions or would like to contribute, please let me know! Andrea Thorn. The collaborators, as of today, are: myself, Yunyun Gao, Kristopher Nolte, Ferdinand Kirsten, Sabrina Stäb (RVZ, University of Würzburg, Germany) Gianluca Santoni (European Synchrotron Facility, France) Tristan Croll (CIMR, University of Cambridge, UK) The Richardson Laboratory (Duke University, USA) We would also like to thank for their advice: Sameer Velankar, James Holton, Manfred Weiss, Gerard Bricogne, Clemens Vonrhein and Robbie Joosten. -- Dr. Andrea Thorn | group leader andrea.thorn(a)uni-wuerzburg.de +49 931 31-83677 Rudolf Virchow Center, University of Wuerzburg Josef-Schneider-Str. 2 | 97080 Wuerzburg | Germany https://www.uni-wuerzburg.de/en/rvz/research/associated-research-groups/tho…

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How to generate LLG map
by afshan begum 26 Mar '20

26 Mar '20

Dear expert, I have collect the data with the bound ligand at 1.4 Å . The ligand contain the sulphate molecule in its ,how could we generate the anamolous signal of sulphate ion to confirm its presence in the structure, actually there are very clear density of the full ligand molecules except for the SO3 ion . As I did it before via phenix but I completely forget it was 4 years ago I used to generate the LLG map for the presence of chloride ion . Many thanks Afshan Sent from my iPhone

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COVID-19 - help design protease inhibitors - 1st round Thurs midnight
by Frank Von Delft 26 Mar '20

26 Mar '20

To all you structural biologists locked out of your labs, bored with answering emails or writing your non-COVID paper, and itching all your lives to be medicinal chemists, here's your chance: https://covid.postera.ai/covid And you get to do something directly on COVID too. It's easy: * stare at the pile of fragments we found bound to the SARS-CoV-2 Main Protease in our somewhat epic XChem fragment screen<https://www.diamond.ac.uk/covid-19/for-scientists/Main-protease-structure-a…> this month (alluded to by others) * see if you can spot cool ways of (especially) merging those hits - or anything else * draw the compound onto that page * hit submit It's actually a bit harder than it sounds - so we're betting that many brains will crack the nut of hitting potency in one go (!). We will do the rest - well, we'll try, if the Filters Approve and the Funds Permit -- and even for that, you can contribute, or tell people that could contribute (details on that page). First collection closes tomorrow (Thurs) midnight Pacific Time (but there will be more). Yes, it is a huge social experiment and a total crapshoot - but we must do something! So thank you for all and any help... *** Do forward to anybody relevant, especially experienced medicinal chemists. *** If you know virology labs set up to do SARS-CoV-2 assays, email the address on that page. *** If you have help to offer or wisdom to share, do so on the forums on that page *** If you want to use the data for anything else - PLEASE DO - we were anxious to push it out ahead of PDB release cycle or getting preprint written. Frank -- Prof Frank von Delft Professor for Structural Chemical Biology Principal Beamline Scientist: I04-1 and XChem Diamond Light Source +44 1235 778997 (office: M,T,T) +44 7471 026103 (mobile) Principal Investigator: Protein Crystallography Structural Genomics Consortium Oxford University +44 1865 617583 (office: W,F)

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Rapid access to COVID-19 related fragment screening
by Fearon, Daren (DLSLtd,RAL,LSCI) 25 Mar '20

25 Mar '20

Dear all, As part of Diamond's effort to combat COVID-19, we are offering fragment screening expertise and infrastructure to users working on COVID-19 related targets (as demonstrated by the recent fragment screening campaign against SAR-CoV-2 Main protease<https://www.diamond.ac.uk/covid-19/for-scientists/Main-protease-structure-a…>). In order to submit a proposal for COVID-19 related research please complete the Rapid Access Form<https://fs3.formsite.com/DiamondLightSource/nynlkya9ks/index.html> and send a completed XChem Application Form<https://www.diamond.ac.uk/dam/jcr:690e7c9d-7b4c-4a7d-bc58-9101e9af4df8/XChe…> to covid19access(a)diamond.ac.uk<mailto:[email protected]>. Due to access and travel restrictions, experienced XChem staff will prepare samples on-site, organise unattended data collection and analyse the data using the XCE pipeline. All data will then be made available to the users and as open access through Fragalysis <https://fragalysis.diamond.ac.uk/viewer/react/landing> and the Diamond webpage. Further details regarding crystal system requirements, available fragment libraries and screening protocols can be found here<https://www.diamond.ac.uk/Instruments/Mx/Fragment-Screening.html>. Kind regards, Daren Dr Daren Fearon XChem Beamline Scientist Diamond Light Source Ltd Harwell Science & Innovation Campus Didcot Oxfordshire OX11 0DE Tel: 01235 778936 Email: daren.fearon(a)diamond.ac.uk<mailto:[email protected]> Web: www.diamond.ac.uk<http://www.diamond.ac.uk/> -- This e-mail and any attachments may contain confidential, copyright and or privileged material, and are for the use of the intended addressee only. If you are not the intended addressee or an authorised recipient of the addressee please notify us of receipt by returning the e-mail and do not use, copy, retain, distribute or disclose the information in or attached to the e-mail. Any opinions expressed within this e-mail are those of the individual and not necessarily of Diamond Light Source Ltd. Diamond Light Source Ltd. cannot guarantee that this e-mail or any attachments are free from viruses and we cannot accept liability for any damage which you may sustain as a result of software viruses which may be transmitted in or with the message. Diamond Light Source Limited (company no. 4375679). Registered in England and Wales with its registered office at Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, United Kingdom

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