- phenixbb - phenix-online.org

Partial occupancy refinement of overlapping inhibitor+water sites
by Matt Jordan McLeod 18 Mar '24

18 Mar '24

Hi all, I am trying to navigate phenix.refine to occupancy refine a partially occupied inhibitor vs. the waters that it displaces. For instance I have molecule resseq 802 in chain A, and waters 1-6 in chain W that are overlapping. When just refining occupancy of the molecule there are clear sites for the waters. How can I refine both of them together so that I can get an occupancy of the molecule vs the group of waters (which should have nearly identical occupancies)? Maybe, a bit more information on the differences in refinement strategy for the occupancy vs fix occupancy vs group occupancy would be more broadly helpful. I tried to make them all a group, but that didn't work as the refinement pushed the waters out and reduced their occupancies to ~0 while leaving the small molecule occupancy about the same as without water. [cid:2b35e3b8-08e5-44ae-9b70-8fdcff613f1a] *Waters are only placed, they are not refined), small molecule is refined to 0.71 occupancy.* -- Matthew Jordan McLeod, PhD Post-Doctoral Fellow | Thorne Lab Cornell University G11 Physical Sciences Building 142 Sciences Drive Ithaca, NY 14853-3501 (607) 279 9382

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uniq segid problem
by jp d 14 Mar '24

14 Mar '24

hi, phenix is crashing with "segid is not unique" problems i have an old job that ran fine in 1.20, in 1.21-5207 i get this (same job script) Sorry: residue.id_str(suppress_segid=false): segid is not unique: pdbres="ALA 65 " segid="PPP " i think the appropriate place in the log is this: Chain: " " Number of atoms: 41993 Number of conformers: 1 Conformer: "" Number of residues, atoms: 1519, 32612 Duplicate atoms: {' A,C1*': 112, ' A,C2': 112, ' A,C2*': 112, ' A,C3*': 112, ' A,C4': 112, ' A,C4*': 112, ' A, C5': 112, ' A,C5*': 112, ' A,C6': 112, ' A,C8': 112, ' A,N1': 112, ' A,N3': 112, ' A,N6': 112, ' A,N7': 112, ' A,N9': 1 12, ' A,O1P': 112, ' A,O2*': 112, ' A,O2P': 112, ' A,O3*': 112, ' A,O4*': 112, ' A,O5*': 112, ' A,P': 112, ' C,C1*': 71 , ' C,C2': 71, ' C,C2*': 71, ' C,C3*': 71, ' C,C4': 71, ' C,C4*': 71, ' C,C5': 71, ' C,C5*': 71, ' C,C6': 71, ' C,N1': 71, ' C,N3': 71, ' C,N4': 71, ' C,O1P': 71, ' C,O2': 71, ' C,O2*': 71, ' C,O2P': 71, ' C,O3*': 71, ' C,O4*': 71, ' C, O5*': 71, ' C,P': 71, ' G,C1*': 179, ' G,C2': 179, ' G,C2*': 179, ' G,C3*': 179, ' G,C4': 179, ' G,C4*': 179, ' G,C5': 179, ' G,C5*': 179, ' G,C6': 179, ' G,C8': 179, ' G,N1': 179, ' G,N2': 179, ' G,N3': 179, ' G,N7': 179, ' G,N9': 179, ' G,O1P': 179, ' G,O2*': 179, ' G,O2P': 179, ' G,O3*': 179, ' G,O4*': 179, ' G,O5*': 179, ' G,O6': 179, ' G,P': 179, ' U,C1*': 69, ' U,C2': 69, ' U,C2*': 69, ' U,C3*': 69, ' U,C4': 69, ' U,C4*': 69, ' U,C5': 69, ' U,C5*': 69, ' U,C6': 69, ' U,N1': 69, ' U,N3': 69, ' U,O1P': 69, ' U,O2': 69, ' U,O2*': 69, ' U,O2P': 69, ' U,O3*': 69, ' U,O4': 69, ' U,O4*': 69, ' U,O5*': 69, ' U,P': 69} Classifications: {'RNA': 1519} Modifications used: {'rna2p': 1, 'rna2p_pur': 82, 'rna2p_pyr': 63, 'rna3p': 10, 'rna3p_pur': 497, 'rna3p_pyr': 444} Link IDs: {'rna2p': 146, 'rna3p': 1372} the 1.20 log does not have these messages and finished normally. maybe a wildcard problem with those stars ? we are not using the '*' in our files has anyone seen that ? should i go back to 1.20 ? or force it to use the 1.20 chem data lib ? thanks jpd

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red blobs
by Andrea Smith 14 Mar '24

14 Mar '24

Hi, i am working on a structure where I have a few relatively big red blobs (please see attached print screens with maps at 1.2 and 3.5 rmsd). The data were processed at BESSY, mtz was used in Phaser and refined in phenix.refine. Can someone explain why this happens (and whether it is an issue)? Thank you, Andrea

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Two-year postdoctoral position in time-resolved crystallography at IBS in Grenoble
by Elke De Zitter 13 Mar '24

13 Mar '24

Dear all, We have an immediate opening for a two-year postdoctoral researcher in SNaX team of the DYNAMOP group at the Institute for Structural Biology in Grenoble (France). The project focuses on the development and optimization of bio-scavengers targeting toxic organophosphorus compounds. The successful candidate will employ time-resolved crystallography and in silico protein design methodologies. The 2-year postdoctoral position is funded by the French National Research Agency via the University Grenoble Alpes, and is open for a young researcher. Applicants must have obtained a Ph.D. in structural biology, biochemistry, biophysics, physics, chemistry, or a related field, no more than three years before the start of the project. The candidate must show a track-record of publications in peer-reviewed journals, and is expected to be proficient in English and highly motivated to learn new skills. The candidate needs to be a good team player as well as being capable of working independently. Experience with one or more of the following skills would be highly evaluated: protein design or the usage of artificial intelligence for structural biology, protein expression and purification, protein crystallization and macromolecular crystallography, serial crystallography, programming or scripting. Interested candidates should apply through the University Grenoble Alpes job portal at https://emploi.univ-grenoble-alpes.fr/job-offers/postdoctoral-researcher-in… (application deadline: 02/04/2024 ). For inquiries regarding the position and application process, please contact Elke De Zitter at elke.de-zitter(a)ibs.fr . All the best, Elke Elke De Zitter Institut de Biologie Structurale - IBS group DYNAMOP 71 avenue des Martyrs 38044 Grenoble Cedex 9, France +33 4 57 42 86 56 elke.de-zitter(a)ibs.fr

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EMBO Workshop on Molecular Neurobiology, 13th to 17th May 2024, Crete
by Jonathan Elegheert 11 Mar '24

11 Mar '24

Dear all, I would like to bring to your attention the EMBO Workshop on Molecular Neurobiology (https://meetings.embo.org/event/24-mol-neurobiology), which will be held from 13th to 17th May 2024 on the beautiful Greek island of Crete, at the Fodele Beach resort (https://www.fodelebeach.gr/). This is a workshop covering the latest breakthroughs in structural biology, biophysics, imaging, and biological models in neurobiology. Given its cross-disciplinary nature, this EMBO workshop presents a broad overview of the field and an insight into the latest technologies and results. It provides a space for learning, for forging new collaborations, and for presenting ideas that will contribute to the future of molecular neurobiology. The workshop also presents an excellent opportunity for early-career scientists to present their work, with a large number of talks that will be selected from submitted abstracts. The workshop poster is attached to this mail, and more information, as well as the registration links, can be found on the following web page; https://meetings.embo.org/event/24-mol-neurobiology The abstract submission deadline is 6th of March. Please do not hesitate to contact me directly for any questions, and we hope to see many of you there! Best wishes, on behalf of the organising committee, Jonathan ----------------------------------------------------------------- Jonathan Elegheert, PhD Team Leader CNRS Scientist Interdisciplinary Institute for NeuroScience (IINS) <https://www.iins.u-bordeaux.fr/> UMR5297 CNRS / UB Centre Broca Nouvelle-Aquitaine 146 rue Léo Saignat BP 61292 33076 Bordeaux Cedex <https://goo.gl/maps/CFNm4dUvzrmmHUM1A> France T: +33 (0)5 33 51 48 57 E: jonathan.elegheert(a)u-bordeaux.fr W: https://www.iins.u-bordeaux.fr/ELEGHEERT Twitter: @ElegheertLab <https://twitter.com/ElegheertLab> -----------------------------------------------------------------

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Issue phenix.table1 macOS
by Xavier Brazzolotto 09 Mar '24

09 Mar '24

I am facing a strange issue with phenix.table1 Previously, I had generated a Table1 with the GUI that was ok. Recently, I have updated to Sonoma 14.4 and when I try to rerun phenix.table1 (or use similar model and with same reflections) do not get consistent results, especially in number of reflections, uniques, CC1/2, CC*... Besides, at the end of a refinement, I do also get an error when the program tries to auto-load the data (model and maps) in Coot… Any thoughts about this Xavier

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Macromolecular Crystallography - CSHL Course October 2024
by Paul Adams 06 Mar '24

06 Mar '24

Dear Colleagues, The Cold Spring Harbor Macromolecular Crystallography course will take place October 13-29th this year (pleased see below for more details). This comprehensive course is an outstanding place to learn both the theoretical and practical aspects of macromolecular crystallography. There are extensive lectures and practical sessions from world recognized experts in crystallization, data collection, data processing, structure solution, refinement, and validation. The goal of the course is for researchers who have had some exposure to structural biology to become experts in crystallography. This is an experience in macromolecular crystallography learning that cannot be found anywhere else, and the student/teacher ratio is often 1:1. Please follow the link below to the course web site. In particular, please note the information about the various fellowships, scholarships, and stipends that are available. If anyone has any questions please send me an e-mail, and we will be happy to answer all queries. Paul Adams <https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…> <https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…> Macromolecular Crystallography <https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…> October 13 - 29, 2024 Applications Due: July 15 Instructors Paul Adams, Lawrence Berkeley National Laboratory Dorothee Liebschner, Lawrence Berkeley National Laboratory Janet Newman, UNSW, Australia James Pflugrath, Rigaku Americas Corporation (ret.), Texas Co-Instructor Tom Peat, UNSW, Australia Topics Covered Basic Diffraction Theory Structure Presentation Coordinate Deposition Structure Validation Model Building and Refinement Electron Density Maps Improvement Using Predicted Models in Structure Solution and Completion Protein Structure Prediction Structure Solution by Experimental Phasing Methods (SAD, MAD, MIR, and others) and Molecular Replacement Data Collection and Processing Synchrotron X-ray Sources and Optics Crystallization (Proteins, Nucleic Acids, Complexes and Membrane Proteins) For further information and to apply please visit the Macromolecular Crystallography course website. <https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…> Cold Spring Harbor Laboratory - Meetings & Courses | 1 Bungtown Road, Cold Spring Harbor, NY 11724 -- Paul Adams (he/him/his) Associate Laboratory Director for Biosciences, LBL (https://biosciences.lbl.gov) 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) Laboratory Research Manager, ENIGMA Science Focus Area (http://enigma.lbl.gov) Adjunct Professor, Department of Bioengineering, UC Berkeley (http://bioeng.berkeley.edu) Member of the Graduate Group in Comparative Biochemistry, UC Berkeley (http://compbiochem.berkeley.edu) Building 91, Room 410 Building 978, Room 4126 Tel: 1-510-486-4225 http://cci.lbl.gov/paul ORCID: 0000-0001-9333-8219 Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 91R0183 Berkeley, CA 94720, USA. Executive Assistant: Michael Espinosa [ MEEspinosa(a)lbl.gov ][ 1-510-333-6788 ] Phenix Consortium: Ashley Dawn [ AshleyDawn(a)lbl.gov ][ 1-510-486-5455 ] --

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map display after resolve_cryoem
by Valerie Biou 01 Mar '24

01 Mar '24

Hello, I ran resolve_cryoem for solvent flattening and obtained a ccp4 map that behaves like a mask both in Coot and Chimera. the histogram is just a single line and the dimensions are different from my original map, even though in a second run I used restore_full_size = true in a second run. To be clear, my original map has 480^3 dimensions, and the output one is 125x140x224, which boxes my protein but I can't see the inside of the map. I guess there is something I didn't understand. Can you please help me? All the best, Valerie Valérie Biou, Ph.D. valerie.biou(a)ibpc.fr Laboratoire de Biologie Physico-Chimique des Protéines Membranaires umr7099.ibpc.fr <http://umr7099.ibpc.fr/> UMR 7099 CNRS/Univ. Paris-Cité Institut de Biologie Physico-Chimique 13 rue Pierre et Marie Curie 75005 Paris - France Tel : +33 (0)1 5841 5099

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Re: [phenixbb] Joint X-ray / neutron refinement
by Kristoffer Lundgren 24 Feb '24

24 Feb '24

Hello phenixbb, When trying to do joint refinement in phenix.refine 1.21-5207 using the suggested joint_xn.eff file found at https://phenix-online.org/documentation/reference/refinement.html#neutron-a… as a template I get some error messages (running phenix.refine from the command line): Unrecognized PHIL parameters: ----------------------------- xray.refinement.refine.strategy (file "joint_xn.eff", line 33) xray.refinement.main.simulated_annealing (file "joint_xn.eff", line 36) xray.refinement.main.ordered_solvent (file "joint_xn.eff", line 37) xray.refinement.main.number_of_macro_cycles (file "joint_xn.eff", line 38) neutron.refinement.refine.strategy (file "joint_xn.eff", line 45) neutron.refinement.main.simulated_annealing (file "joint_xn.eff", line 48) neutron.refinement.main.ordered_solvent (file "joint_xn.eff", line 49) neutron.refinement.main.number_of_macro_cycles (file "joint_xn.eff", line 50) Can you please advice on how to proceed? It looks like the options supplied are not recognized at all by phenix.refine. Best regards Kristoffer From: <phenixbb-bounces(a)phenix-online.org> on behalf of Derek Logan <derek.logan(a)biochemistry.lu.se> Date: Monday, 22 January 2024 at 09:39 To: "phenixbb(a)phenix-online.org" <phenixbb(a)phenix-online.org> Cc: Ulf Ryde <ulf.ryde(a)compchem.lu.se>, "esko.oksanen_ess.eu" <esko.oksanen(a)ess.eu> Subject: ***SPAM*** [phenixbb] Joint X-ray / neutron refinement Hi phenixbb, I'm trying to understand the current status of joint X-ray/neutron refinement in phenix.refine. The announcement of the latest release mentions a change in the algorithm as described in the recent publication. In the documentation: Structure refinement in PHENIX<https://phenix-online.org/documentation/reference/refinement.html#neutron-a…> phenix-online.org<https://phenix-online.org/documentation/reference/refinement.html#neutron-a…> [AURqZhI53yp3gAAAABJRU5ErkJggg==]<https://phenix-online.org/documentation/reference/refinement.html#neutron-a…> it's described how you can run joint refinement using a parameter file. Does this mean that it is *only* possible in this way and not through the GUI? The GUI was very useful in the past as it automatically opened Coot with the maps for both X-rays and neutrons, and the refinement statistics for both were displayed in the GUI. As far as I can see joint refinement via the GUI last worked in version 1.19.2-4148 from 2021. Best regards Derek

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Rotamer error in real space refinement
by Nikos Pinotsis 23 Feb '24

23 Feb '24

Hi, I am using real space refine with the latest phenix 1.21-5207 for fitting a model into a cryoEM map. During refiment one Trp goes clearly out of density (vertical to the density) although the map is very well defined at this part of the protein. I tried local_grid_search either for every cycle or last, however it didn't fix the problem. I know that this is reported a couple of years ago as fixed (dev-4218), I am wondering if something changed during the last version. Another solution I can think it to keep the side chain of this Trp fixed. How can I do that? thanks Nikos -- ________________________________________ Nikos Pinotsis Associate Professor Biochemistry, Department of Chemistry National and Kapodistrian University of Athens

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