- phenixbb - phenix-online.org

Phenix, MolProbity, and Amber
by Eric Williams 30 Jul '19

30 Jul '19

Greetings, all I'm trying to run the MolProbity programs (reduce, ramalyze, etc) in Phenix 1.16-3649, and I get the following warning: "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" I do not recall seeing that in earlier versions. Do I need to worry about it? If so, how do I fix it? Thanks. :) Eric

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General interest
by John R Helliwell 30 Jul '19

30 Jul '19

Dear Colleagues, For your general interest, you can find the lecture slides that I presented at ACA 2019 in the Transactions Symposium on Data via the weblink here:- https://forums.iucr.org/viewtopic.php?f=39&t=421 Best wishes, John Emeritus Professor John R Helliwell DSc Chairman of IUCr CommDat

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ISOLDE dev builds now available
by Tristan Croll 30 Jul '19

30 Jul '19

Hi all, Since the release of ISOLDE 1.0b3 I've begun releasing regular (weekly~fortnightly) development builds of ISOLDE. These are built against the ChimeraX daily build at the time of release - if you download a ChimeraX-daily build and install ISOLDE in the usual way via Tools/More Tools... this is what you'll get. In case you're worried, the dev and official 1.0b3 builds install into different directories, so it's quite straightforward to have both versions running independently on the same machine. The dev builds are *not* compatible with the ChimeraX 0.9 stable release. Some important changes since 1.0b3/ChimeraX 0.9: - the ChimeraX team have fixed some bugs affecting PDB and mmCIF I/O (primarily involving the handling of "imperfect" files) - fixed a bug causing the simulation to crash if the minimiser didn't converge in the first round - added status messages during simulation startup, and clear indications of when a simulation is running/paused - improved simulation startup time, and handling of custom ligands (preparing ligand definition files is a work in progress and will currently need you to do some work outside ISOLDE - feel free to contact me if you have an urgent case) Best regards, Tristan

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modify.remove option in phenix.refine
by wtempel 29 Jul '19

29 Jul '19

Hi, for calculation of an omit map, with the atoms in question fully removed from the model, I experimented with the modify_start_model.modify.remove option and got: ====================== Modifying start model if requested ===================== Size before: 505 size after: 491 Traceback (most recent call last): File "/home/user1/phenix-1.16-3549/build/../modules/phenix/phenix/command_line/refine.py", line 11, in command_line.run(command_name="phenix.refine", args=sys.argv[1:]) File "/home/user1/phenix-1.16-3549/modules/phenix/phenix/refinement/command_line.py", line 106, in run log=log) File "/home/user1/phenix-1.16-3549/modules/phenix/phenix/refinement/driver.py", line 271, in __init__ self.model.set_xray_structure(modify_model_obj.xray_structure) File "/home/user1/phenix-1.16-3549/modules/cctbx_project/mmtbx/model/model.py", line 693, in set_xray_structure self.set_sites_cart_from_xrs() File "/home/user1/phenix-1.16-3549/modules/cctbx_project/mmtbx/model/model.py", line 1722, in set_sites_cart_from_xrs self._pdb_hierarchy.adopt_xray_structure(self._xray_structure) File "/home/user1/phenix-1.16-3549/modules/cctbx_project/iotbx/pdb/hierarchy.py", line 688, in adopt_xray_structure raise RuntimeError("Incompatible size of hierarchy and scatterers array.") RuntimeError: Incompatible size of hierarchy and scatterers array. I verified that my intended selection indeed comprises 14 atoms. Has anyone used the remove option inside phenix.refine successfully. Thanks. Wolfram Tempel

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cbf to sfrm
by Tim Gruene 28 Jul '19

28 Jul '19

Dear all, recently the conversion from CBF to SFRM frame format with APEX was discussed on the Bruker mailing list ("Synchrotron data with Bruker Software"), including a potential bug that parameters in the frames other than the first frame are not set correctly. The workaround to re-convert from SFRM to SFRM a second time did not help in my case. I therefore updated my program sfrmtools, available at https:// homepage.univie.ac.at/tim.gruene/research/programs/conv/sfrmtools/ With the option '-u',you can provide the first frame of the run, and via '-p' a parameter file that contains the critical parameters (see documentation at above URL) to update the header for all frames in this run. In case you have twinned data and want to benefit from SAINT, this should be possible with this feature. Both 64bit Linux binary and the source code are available. The program has no dependencies and should compile under any platform. I did not debug this new feature very thoroughly, but it worked for me so far. Any bug reports are welcome to this address tim.gruene(a)univie.ac.at I hope this is helpful for one or two users. I acknowledge the thorough documentation of XDS, of SAINT, and of the SFRM header format. Kind regards, Tim cc Bruker mailing list, CCP4BB, phenixBB -- -- Tim Gruene Head of the Centre for X-ray Structure Analysis Faculty of Chemistry University of Vienna Phone: +43-1-4277-70202 GPG Key ID = A46BEE1A

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Unwanted LINK records
by Luca Pellegrini 27 Jul '19

27 Jul '19

Hello, Phenix.real_space_refine generates a few spurious covalent bonds between protein and ligand in my structure, which distort the local structure, and then adds the corresponding LINK records in the output file. Is there a way to avoid this? I am aware of the anti-link option previously mentioned in the phenixbb: http://www.phenix-online.org/pipermail/phenixbb/2018-January/023677.html, but I was wondering if there was another way of preventing this from happening. I am using Phenix 1.15.2-3472. Best wishes, Luca Luca Pellegrini, PhD Department of Biochemistry University of Cambridge Cambridge CB2 1GA United Kingdom lp212(a)cam.ac.uk tel.: 0044 1223 760469 https://www.bioc.cam.ac.uk/pellegrini-group/pellegrini-group @PellegriniLab

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Symmetry of map vs Symmetry of model
by pramod kumar 26 Jul '19

26 Jul '19

Dear all, I have a query related to symmetry imposition and corresponding tweaking of model. If symmetry (say, C4) was imposed during the reconstruction of a 3D volume, does symmetry also need to be imposed when building the atomic model (say, in Phenix)? Or could this constrain be relaxed? Do we need to tweak the model in Coot for other chains or since it is build on symmetrical partners therefore should only be made in one chain and copied for all without any fitting? Pramod Jaykar, Ph.D.

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Re: [phenixbb] Unwanted LINK records
by Dale Kreitler 26 Jul '19

26 Jul '19

Hi Luca, Try running with the parameter: refinement.pdb_interpretation.automatic_linking.link_ligands=False Check if automatic linking is enabled with the All parameters button in the GUI. Looks like the default might be True? -D On Fri, Jul 26, 2019 at 11:21 AM Luca Pellegrini <lp212(a)cam.ac.uk> wrote: > Hello, > > Phenix.real_space_refine generates a few spurious covalent bonds between > protein and ligand in my structure, which distort the local structure, and > then adds the corresponding LINK records in the output file. Is there a way > to avoid this? > > I am aware of the anti-link option previously mentioned in the phenixbb: > http://www.phenix-online.org/pipermail/phenixbb/2018-January/023677.html, > but I was wondering if there was another way of preventing this from > happening. I am using Phenix 1.15.2-3472. > > Best wishes, > Luca > > Luca Pellegrini, PhD > Department of Biochemistry > University of Cambridge > Cambridge CB2 1GA > United Kingdom > > lp212(a)cam.ac.uk > tel.: 0044 1223 760469 > https://www.bioc.cam.ac.uk/pellegrini-group/pellegrini-group > @PellegriniLab > > > > _______________________________________________ > phenixbb mailing list > phenixbb(a)phenix-online.org > http://phenix-online.org/mailman/listinfo/phenixbb > Unsubscribe: phenixbb-leave(a)phenix-online.org > -- Dale Kreitler Graduate Research Assistant Gellman Lab Department of Chemistry University of Wisconsin-Madison

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Symmetry of map Vs Symmetry of model
by pramod kumar 26 Jul '19

26 Jul '19

Dear all, I have a query related to symmetry imposition and corresponding tweaking of model. If symmetry (say, C4) was imposed during the reconstruction of a 3D volume, does symmetry also need to be imposed when building the atomic model (say, in Phenix)? Or could this constrain be relaxed? Do we need to tweak the model in Coot for other chains or since it is build on symmetrical partners therefore should only be made in one chain and copied for all without any fitting? Pramod Jaykar, Ph.D.

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CryoEM specialist positions open at CSIR-CCMB, India
by Rukmini Raju 22 Jul '19

22 Jul '19

Dear All, This is to bring to your kind attention two vacancies for Structural Biologists with CryoEM expertise at the CCMB, Hyderabad, India. CSIR-Centre for Cellular and Molecular Biology, Hyderabad (CSIR-CCMB) is a Premier Research Laboratory under the Council of Scientific & Industrial Research (CSIR), involved in multidisciplinary R&D programmes of both basic and applied nature across scientific disciplines of biological sciences. The link for the application is given below: http://www.ccmb.res.in/index.php?view=notifications&mid=0&id=71&nid=268 Best regards, Sankar -- ****************************************************************************** Dr. Rajan Sankaranarayanan Chief Scientist, Structural Biology Laboratory CSIR-Centre for Cellular and Molecular Biology (CCMB) Uppal Road Hyderabad - 500 007 India. Ph: +91-(0)40 2719 2832 to 2835 (Lab) +91-(0)40 2719 2500 (CCMB Reception) Fax: +91-(0)40 2716 0252, 2716 0591 e-mail: sankar(a)ccmb.res.in sankarfr(a)yahoo.com Web: http://e-portal.ccmb.res.in/e-space/sankar/index.html ******************************************************************************** -- ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ R. Rukmini Principal Technical Officer Structural Biology, R-100, R&D Building CSIR-Centre for Cellular and Molecular Biology Uppal Road, Hyderabad - 500 007 India Phone# +91-40-27192953(callto:+91-40-27192953) (R-100) +91-40-27192835(callto:+91-40-27192835) (Lab, Main Building) ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~

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Real space refinment keeps messing up my taxol conformation
by Ahmad Khalifa 20 Jul '19

20 Jul '19

I used elbow to generate restraints for taxol using chemical componenet and sdf file. I posted before to the list and Oleg was kind enough to provide restraints generated by readyset. No matter what restraints I use, the taxol is messed up! The other thing is, the refinement keeps breaking the peptide bond at a specific location! I would like to send some files to someone privately to investigate! Please let me know. Regards.

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phenix.pdbtools
by Raja Dey 18 Jul '19

18 Jul '19

Dear Members, I like to regularize the geometry of selected residues' side chains using phenix.pdbtools? I couldn't find the syntax. I used the following command line syntax, but didn't work. Can someone help correcting this command? phenix.pdbtools myprotein.pdb geometry-regularization=true selection="((chain A and ((resseq 236:237 not backbone) or (resseq 240:241 not backbone) or (resseq 244 not backbone) or (resseq 254 not backbone) or (resseq 258 not backbone) or (resseq 261:262 not backbone) or (resseq 412:413 not backbone) or (resseq 416:417 not backbone) or (resseq 419 not backbone))) or (chain X and ((resseq 104 not backbone) or (resseq 107:108 not backbone) or (resseq 111 not backbone) or (resseq 113 not backbone)))) Best regards, Raja

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Understanding Biology through Structure, March 16-20, 2020 in Santa Fe, NM
by Tom Terwilliger 18 Jul '19

18 Jul '19

Hi Structural biologists, particularly students and postdocs! I hope that you can come to our second "Understanding Biology through Structure” conference, to be held in Santa Fe, NM March 16-20, 2020. The purpose of the conference is to provide a forum for students and postdocs to meet established researchers as well as some rising stars, and to see and discuss presentations on the latest methods and results. The last conference was a huge success (see https://bit.ly/2Gfkm4t and https://bit.ly/2Gg39rm) and this one is looking great (see https://cvent.me/4kq9P) We have a super group of speakers (keynote speakers are Ilme Schlichting, David Stuart, Erica Ollmann Saphire, Robert Stroud, Suzanne Scarlata, David Eisenberg, Wayne Hendrickson, Yvonne Jones, Eva Nogales, and Tom Blundell), and all the talks will be followed by 10-15 minutes of discussion with participation by students and postdocs especially encouraged. There are a number of fellowships covering hotel and registration available for students and postdocs. Successful applicants will be notified on a rolling basis about a month after they register for the conference. After the main conference there will be an optional Phenix workshop with lectures and hands-on sessions on using Phenix for crystallography and cryo-EM. You can register now at https://cvent.me/4kq9P ! Best regards, Tom T -- Thomas C Terwilliger Laboratory Fellow, Los Alamos National Laboratory Senior Scientist, New Mexico Consortium 100 Entrada Dr, Los Alamos, NM 87544 Email: tterwilliger(a)newmexicoconsortium.org Tel: 505-431-0010

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Broken Phenix Coot integration after upgrade to v 1.16
by Ahmad Khalifa 17 Jul '19

17 Jul '19

Hello, After the update, when I open coot from validation with Phenix integration, and navigate to different atoms, clashes, etc, I get moved to an empty space outside of my map and model. What's going wrong here? Regards.

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Phenix real space refine problems
by Gyles Cozier 16 Jul '19

16 Jul '19

Good afternoon, I have been having issues with the last 3 versions of Phenix (1.14, 1.15 and 1.16) when the XYZ(real-space) option is selected, version 1.13 was the last one that doesn't have this problem for me. This seems to place too much weight on correcting rotamer 'outliers' at the expense of fitting to the density. The proteins that I work on have always had some residues that consistently are identified as rotamer outliers, but these latest versions 'correct' just about all of them (typically from 1% down to 0.1%). The resulting structures show clear movement of the sidechains out of what should be their density. Image 1 (after using 1.13) and 2 (after using 1.14, 1.15 or 1.16) show a really bad example where the Arg sidechain even gets broken apart to be moved into the stronger density of a neighbouring symmetry Gln. Image 3 (after using 1.13) and 4 (after using 1.14, 1.15 or 1.16) is a more subtle example, but although the residue is no longer a rotamer outlier after refinement using 1.16, it clearly does not fit the density as well as after using 1.13. These subtle changes are particularly worrying, as they could easily be missed when checking the structure after refinement. Other members of the group have also noticed this problem for different proteins. So currently I have a choice of either using version 1.13 (which with Onedep no longer accepting pdb files makes things a bit inconvenient as is nice to use the latest version for getting the mmcif and validation), or to use 1.16, but switch off the XYZ(real-space). Has anyone else noticed this happening? Found a solution to the problem? Thank you for any suggestions, Gyles Cozier.

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upgrading phenix version on linux
by Ahmad Khalifa 15 Jul '19

15 Jul '19

Hello, How should I upgrade my Phenix installation? Remove the old one first, or install to a different directory keeping both? Does the new installation take care of it already?! Regards.

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Berkeley Web Services Downtime
by Paul Adams 13 Jul '19

13 Jul '19

Dear Colleagues, as a result of electrical work at LBNL the following servers will be unavailable over the weekend: - 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/) We expect that the servers will be available some time on Monday July 15th. 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. Cheers, Paul -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley Lab (http://biosciences.lbl.gov/divisions/mbib) Division Deputy for Biosciences, Advanced Light Source, Lawrence Berkeley Lab (https://als.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) Vice President for Technology, the Joint BioEnergy Institute (http://www.jbei.org) Laboratory Research Manager, ENIGMA Science Focus Area (http://enigma.lbl.gov) 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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Opportunity in the Gonen lab
by Johan Hattne 13 Jul '19

13 Jul '19

Dear all; There is an exciting opportunity for a research technician to join the Gonen lab at UCLA, supporting ongoing projects in membrane biophysics and biochemistry. This role will perform research using biochemical and molecular biology techniques. The Gonen Lab at the University of California works toward understanding how membrane proteins help cells maintain homeostasis. To that end we study channels, transporters, and receptors structurally and functionally. Complete job posting and application instructions can be found at: https://hhmi-openhire.silkroad.com/epostings/index.cfm?fuseaction=app.jobin… // Best wishes; Johan Research Specialist @ Gonen Lab ____________________________________________________ UCLA * 615 Charles E. Young Drive South BSRB #347 * Los Angeles, CA 90095

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High B factors
by ssolmaz 12 Jul '19

12 Jul '19

Dear Kay, Thank you, this is helpful. Yes, the data were collected at the synchrotron with a Dectris Pilatus 6MF detector. CC1/2 at the highest resolution shell (2.55A - 2.5A) is 0.481 and I/sigma(I) is 1.2. The multiplicity is 9.7. Best, Sozanne. Sozanne Solmaz, Ph. D. Assistant Professor of Biological Chemistry Department of Chemistry, State University of New York at Binghamton PO Box 6000, Binghamton, NY 13902 Office: Smart Energy Building Room SN1045 25 Murray Hill Road, Vestal, NY, 13850 http://chemiris.chem.binghamton.edu/SOLMAZ/solmaz.html

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Re: [phenixbb] High B factors
by Kay Diederichs 12 Jul '19

12 Jul '19

Dear Sozanne, I expect these data were collected at a synchrotron, and they are quite weak at 2.5A? (would be good to know CC1/2 in the high-resolution shell) If so, what you see is normal, and there's most likely nothing wrong with your data or model. I've seen Wilson and average B-factors higher than the ones you cite, for perfectly correct models and well-measured data. It is just a fact that your protein's atoms vibrate in the lattice, and the B factors are a way to measure how much. There is a mathematical relation between B-factors and strength of diffraction at high resolution; the higher the former, the lower the latter. best, Kay On 7/11/19 6:49 PM, phenixbb-request(a)phenix-online.org wrote: > Date: Thu, 11 Jul 2019 11:50:52 -0400 > From: ssolmaz <ssolmaz(a)binghamton.edu> > To: phenixbb(a)phenix-online.org > Subject: [phenixbb] High B factors > Message-ID: > <CAHYfRfKKMViLmaEuVr0aANGu6iaW6ofMAWSKHZ5JuCnOusFQ4w(a)mail.gmail.com> > Content-Type: text/plain; charset="utf-8" > > Dear all, > We recently determined a protein structure by molecular replacement and the > statistics are looking good, however, the average B-factor is unusually > high, and the Wilson B-factor is high too. A quick research on the subject > suggested that high B-factors are acceptable as long as one has excluded > and double-checked for other crystallographic problems. Which problems > should I check for and what is your opinion on the high B-factor? Is there > anything that could be done to lower it? > > Resolution: 2.5 A > Space group P3121, 60.0 60.0 142.6 90 90 120 > R work 24.6% > R free 26.4% > Wilson B-factor 73.2 > Average B-factor 99.5 > > Thank you for your advice, > Best, Sozanne. > > Sozanne Solmaz, Ph. D. > Assistant Professor of Biological Chemistry > Department of Chemistry, State University of New York at Binghamton > PO Box 6000, Binghamton, NY 13902 > Office: Smart Energy Building Room SN1045 > 25 Murray Hill Road, Vestal, NY, 13850 > http://chemiris.chem.binghamton.edu/SOLMAZ/solmaz.html -- Kay Diederichs http://strucbio.biologie.uni-konstanz.de email: Kay.Diederichs(a)uni-konstanz.de Tel +49 7531 88 4049 Fax 3183 Fachbereich Biologie, Universität Konstanz, Box M647, D-78457 Konstanz This e-mail is digitally signed. If your e-mail client does not have the necessary capabilities, just ignore the attached signature "smime.p7s".

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Comprehensive validation fatal problems interpreting model
by Ahmad Khalifa 11 Jul '19

11 Jul '19

Hello, I have a fatal error with my model regarding a number of atoms with unknown nonbonded energy type symbol! I attached a screenshot of the error and my pdb, can you please help me debug the problem? Best regards.

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Phenix website, servers and bulletin board
by Nigel Moriarty 11 Jul '19

11 Jul '19

Folks Due to the rerouting of 12kV underground transmission lines near our building, there will interruptions to Phenix computer services starting 12 July for about a week. The plan calls for only short outages but please be prepared for anything. 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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High B factors
by ssolmaz 11 Jul '19

11 Jul '19

Dear all, We recently determined a protein structure by molecular replacement and the statistics are looking good, however, the average B-factor is unusually high, and the Wilson B-factor is high too. A quick research on the subject suggested that high B-factors are acceptable as long as one has excluded and double-checked for other crystallographic problems. Which problems should I check for and what is your opinion on the high B-factor? Is there anything that could be done to lower it? Resolution: 2.5 A Space group P3121, 60.0 60.0 142.6 90 90 120 R work 24.6% R free 26.4% Wilson B-factor 73.2 Average B-factor 99.5 Thank you for your advice, Best, Sozanne. Sozanne Solmaz, Ph. D. Assistant Professor of Biological Chemistry Department of Chemistry, State University of New York at Binghamton PO Box 6000, Binghamton, NY 13902 Office: Smart Energy Building Room SN1045 25 Murray Hill Road, Vestal, NY, 13850 http://chemiris.chem.binghamton.edu/SOLMAZ/solmaz.html

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exclude atoms/regions in real space refinement
by Filip Van Petegem 04 Jul '19

04 Jul '19

Dear Phenix users, I want to exclude particular regions of a protein model, docked into a cryo-EM map, from real-space refinement. I know this is possible for refinement in reciprocal space, but is this possible for refining a cryo-EM structure against a map? E.g. I want to totally exclude a region with known crystal structure, placed in an area of poor local resolution, from any form of refinement, but want to apply all other options (morphing, simulated annealing, adp, Global minimization) to the remainder of the structure. (I didn't see this option in https://www.phenix-online.org/documentation/reference/real_space_refine.html ) best regards, Filip -- Filip Van Petegem, PhD Professor, Dept. of Biochemistry and Molecular Biology The University of British Columbia 2350 Health Sciences Mall - Rm 2.356 Vancouver, V6T 1Z3 phone: +1 604 827 4267 email: filip.vanpetegem(a)gmail.com http://crg.ubc.ca/VanPetegem/

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AUC2019. Registrations still open. Graduate and Postdoctoral scholarship awards available.
by Renwick Dobson 03 Jul '19

03 Jul '19

Dear Structural biology community, AUC2019<https://auc2019.uleth.ca/>, the 24th AUC Workshop and Symposium, will be held at the University of Canterbury, Christchurch (New Zealand) from 24-29 August 2019. 1) Registrations are now open and details can be found at this website: https://auc2019.uleth.ca/. Early Bird Registrations have been extended to the 15th July. 2) Beckman Coulter Life Sciences is generously offering one scholarship to a Graduate student and one to a Postdoctoral fellow to attend AUC2019 in Christchurch, New Zealand. Awardees will have their transportation (including airfare) and registration to the symposium and workshops covered (to a value of $1500USD). In addition, awardees will give a short talk in the symposium on their research. If you are interested, please submit the following to Ren Dobson (renwick.dobson(a)canterbury.ac.nz<mailto:[email protected]>) by the 18th July: i) a 400 word summary on how AUC has been used in your research, or alternatively, how you intend to use AUC during your research. (in pdf format) ii) A CV (in pdf format) iii) a scientific abstract for the talk. A template for the abstract is here: https://www.dropbox.com/s/sccrqoyp9wo7alm/NZ.AUC2019_AUC_SampleAbstract_for…. (submit in pdf format) Note, deadline for the Beckman Coulter Scholarships is the 18th July. The winners will be announced by the 31st July. 3) As the scientific program<https://auc2019.uleth.ca/symposium.php> for AUC2019 emerges, events will be uploaded to the website. We strongly encourage you to submit abstracts for talks and posters<https://auc2019.uleth.ca/abstracts.php>. 4) The format of the event is a 2-3 day workshop<https://auc2019.uleth.ca/workshops.php> offering parallel, hands-on training in experimental design and the latest AUC data analysis software from the world experts in this area followed by a 2 day research symposium on AUC and complementary approaches: methodological development, combination with orthogonal techniques (SAXS, SANS, SPR, MST, SEC-MALLS etc), application in biosciences and material sciences. 5) The meeting is also timed such that delegates can also attend the Biomolecular interactions and Engineering Symposium<https://www.queenstownresearchweek.org/bio-interactions/>, which is part of the Queenstown Molecular Biology Conference (this is in Queenstown, NZ), although note that this is a separate conference. 6) Lastly, The European Biophysics Journal has kindly agreed to run a special issue to celebrate the research presented at AUC2019. Therefore, we invite those who wish to extend their talks to a journal publication to consider contributing original research articles to this issue. Please indicate your interest for inclusion in this volume below. Deadline for registration of a contribution is August 30 2019. We look forward to welcoming you to Christchurch, New Zealand next Spring(-ish)! Ren Dobson, Chair AUC2019 On behalf of the AUC2019 Scientific Organising Committee ---- Prof. Ren Dobson Co-Director, Biomolecular Interaction Centre (BIC) http://www.bic.canterbury.ac.nz/ School of Biological Sciences | Te Kura Pūtaiao Koiora University of Canterbury | Te Whare Wānanga o Waitaha Private Bag 4800 Christchurch | Ōtautahi New Zealand | Aotearoa E: renwick.dobson(a)canterbury.ac.nz<mailto:[email protected]> T: ++64 (03) 369-5145 x 95145 F: ++64 (03) 364-2590 W: http://dobsonlab.org/

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