- phenixbb - phenix-online.org

ImportError: This package should not be accessible on Python 3. Either you are trying to run from the python-future src folder or your installation of python-future is corrupted.
by Darin Lory 20 May '19

20 May '19

Phenix Gurus, I'm trying to setup PyMOL(TM) 2.3.2 with Phenix 1.15.2-3472. My pymol is installed in file /apps/packages/pymol/pymol /apps/packages/pymol/pymol: symbolic link to `bin/pymol' I setup in Phenix -> Preferences -> Graphics -> PyMol Path as /apps/packages/pymol/bin/pymol. Any ideas why this is happening? My source file is /apps/packages/phenix/phenix-1.15.2-3472/phenix_env.sh #!/bin/sh # export PHENIX="/apps/packages/phenix/phenix-1.15.2-3472" export PHENIX_VERSION=1.15.2-3472 . $PHENIX/build/setpaths.sh ++++++++++++++ ++++++++++++++ phenix Already checked for new versions in last 24 hours, skipping Could not import runpy module Traceback (most recent call last): File "/apps/packages/pymol/lib/python3.7/runpy.py", line 15, in <module> import importlib.util File "/apps/packages/pymol/lib/python3.7/importlib/util.py", line 14, in <module> from contextlib import contextmanager File "/apps/packages/pymol/lib/python3.7/contextlib.py", line 5, in <module> from collections import deque File "/apps/packages/pymol/lib/python3.7/collections/__init__.py", line 27, in <module> from reprlib import recursive_repr as _recursive_repr File "/apps/packages/phenix/phenix-1.15.2-3472/conda_base/lib/python2.7/site-packages/reprlib/__init__.py", line 7, in <module> raise ImportError('This package should not be accessible on Python 3. ' ImportError: This package should not be accessible on Python 3. Either you are trying to run from the python-future src folder or your installation of python-future is corrupted. Best regards, -Darin "The most exciting phrase to hear in science, the one that heralds new discoveries, is not 'Eureka!' (I found it!) but 'That's funny ...'" -Issac Asimov [image: --] Darin S. Lory [image: https://]about.me/darin.lory <https://about.me/darin.lory?promo=email_sig&utm_source=email_sig&utm_medium…>

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minimizing clash score
by Titus, Erron 18 May '19

18 May '19

Hello, In order to improve model geometry of my x-ray structure, I am using real-space refinement together with reciprocal space refinement in phenix.refine. I like this, because it works very well to fix a lot of geometry issues. But clashes are a problem. Clashes tend to keep coming back. I found a clunky way to selectively use reference restraints to prevent most of the clashes from coming back, but I am wondering if there is another way of addressing this. I don't want to up-weight geometry globally, because 1) there are major regions of the x-ray map that are quite good, and 2) I don't have problems with other geometry, just clashes. I couldn't find much documentation on the "clash_guard" keyword... Thanks. Erron

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Re: [phenixbb] minimizing clash score
by oleg＠quantumbioinc.com 17 May '19

17 May '19

Dear Erron, We recently demonstrated that the high clash count typically seen with the conventional PHENIX refinement is likely attributed to a particular non bonded restraint function used by phenix.refine. When we employed QM/MM (ONIOM) refinement (Borbulevych et al., Acta Cryst., 2018, D74, 1063 https://doi.org/10.1107/S2059798318012913 ) that resulted in significantly better clashscore and improvements of other metrics. QM/MM refinement is available within PHENIX with the DivCon plugin. This plugin is available at no cost to academic users at http://www.quantumbioinc.com/products/software_licensing. Sincerely, Oleg Borbulevych Oleg Borbulevych, Ph.D. Staff Scientist QuantumBio, Inc. 2790 W. College Ave. State College, PA 16801 E-mail: oborbulevych(a)yahoo.com, oleg(a)quantumbioinc.com Linkedin Professional Profile: https://www.linkedin.com/in/oleg-borbulevych-b8045422 -----Original Message----- From: "Titus, Erron" <Erron.Titus(a)ucsf.edu> Sent: Friday, May 17, 2019 1:58pm To: "phenixbb(a)phenix-online.org" <phenixbb(a)phenix-online.org> Subject: [phenixbb] minimizing clash score _______________________________________________ phenixbb mailing list phenixbb(a)phenix-online.org http://phenix-online.org/mailman/listinfo/phenixbb Unsubscribe: phenixbb-leave(a)phenix-online.orgHello, In order to improve model geometry of my x-ray structure, I am using real-space refinement together with reciprocal space refinement in phenix.refine. I like this, because it works very well to fix a lot of geometry issues. But clashes are a problem. Clashes tend to keep coming back. I found a clunky way to selectively use reference restraints to prevent most of the clashes from coming back, but I am wondering if there is another way of addressing this. I don't want to up-weight geometry globally, because 1) there are major regions of the x-ray map that are quite good, and 2) I don't have problems with other geometry, just clashes. I couldn't find much documentation on the "clash_guard" keyword... Thanks. Erron

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Dots and vectors of cryo em validation in Coot
by Ahmad Khalifa 17 May '19

17 May '19

Hello, In the manual, it says the red dots are clashes, what about the yellow dots and the magenta dashes (vectors)? I would also appreciate if you give an input on how you fix them. Best regards.

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On estimating Unitary Structure Factor distribution
by Andre LB Ambrosio 15 May '19

15 May '19

Dear all, We seek to calculate the distribution of Unitary Structure Factors, Uhkl, from a few datasets (at different maximum resolutions) for which the corresponding atomic models are already available at the PDB; this according to the formula (6.4), in the 2nd edition of Jan Drenth´s book: Uhkl = exp[B*(sin^2(theta)/lambda^2)] x FOBShkl / F(000) Hence, the following questions: - Is there any macromolecular crystallography software that can compute Uhkl as above, or equivalent? - If not, would it be more correct to use the Wilson-B or the mean B from the final model? - How can F(000) be best estimated from the final model, which is not necessarily always the most complete or best refined? Should we simply add together the number of electrons for all the atoms refined in the asymmetric unit (protein + ligands + solvent)? Many thanks in advance and best wishes, -- Andre LB Ambrosio

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Postdoctoral Research Assistant at University of Dundee (Alessio Ciulli)
by KH Chan 15 May '19

15 May '19

Posting on behalf of Prof. Alessio Ciulli: Professor Alessio Ciulli’s laboratory is seeking a postdoctoral researcher to undertake research in collaboration with one of the leading pharmaceutical companies supporting the Division of Signal Transduction Therapy (DSTT). The DSTT facilitates collaborations between some of the world’s major pharmaceutical companies (Boehringer Ingelheim, GlaxoSmithKline, and Merck-Serono) and leading Dundee-based researchers with a proven track record of achievement in understanding and exploiting the fundamental molecular causes of human disease in the fields of cancer, immune-regulation, neurodegeneration and hypertension resulting from disruptions in protein ubiquitylation, phosphorylation and other signalling networks. The successful applicant will be based within the Ciulli lab in Dundee ( http://www.lifesci.dundee.ac.uk/groups/alessio-ciulli). The laboratory is pioneering novel chemical structural biology approaches to target E3 ubiquitin ligases with small molecules. The applicant will employ state of the art structural biology, cell biology and biophysical approaches to conduct molecular and structural studies on disease-relevant human E3 ubiquitin ligases. The Ciulli lab has close collaborations and access to facilities available within both the MRC Protein Phosphorylation Unit ( http://www.ppu.mrc.ac.uk/) and more widely within the School of Life Sciences. This set-up will ensure the successful candidate will have access to whatever technologies required to conduct the projects that they are working on, including molecular, biochemical, mass spec proteomics, pharmacological and genetic methodologies including CRISPR/CAS9 knock-out and knock-in technologies. There will be regular opportunity for interaction and to discuss data within the group and with the collaborating pharma company. Candidate requirements: ‧ PhD with outstanding academic track record and at least one first authored publication in an internationally recognised peer-reviewed journal. ‧ Strong background in Biochemistry, Molecular Cell Biology, or Structural Biology is required. ‧ Strong interest in signal transduction research and how disruptions of these pathways are linked to human disease is expected. ‧ Experience with recombinant protein expression and purification, molecular cloning, and protein X-ray crystallography (or cryo-EM) is required. ‧ Experience with mammalian cells tissue culture, and protein-protein interaction studies inside cells e.g. pull-down, proteomics, would be highly advantageous. ‧ Experience with biophysical methods to study in vitro protein-protein and protein-peptide interactions is desirable. ‧ Capable of working in a team, but able to plan and work independently. ‧ Excellent communication skills and knowledge of the English language are essential. ‧ The candidate should have ambitions to become a successful independent researcher either in academia or the pharmaceutical/biotechnology industry. The fund for this project is available till 30th June 2020 in the first instance with a chance to renew. For informal enquiries please contact Prof Alessio Ciulli a.ciulli(a)dundee.ac.uk or Dr Kwok-Ho Chan k.chan(a)dundee.ac.uk Closing Date 31 May 2019 Job details: https://ig5.i-grasp.com/fe/tpl_uod01.asp?newms=jj&id=103176&newlang=1

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Research Associate (Fixed Term) at the MRC Mitochondrial Biology Unit, University of Cambridge
by Jonathan Ruprecht 15 May '19

15 May '19

Posting on behalf of Dr Edmund Kunji: The University of Cambridge wishes to appoint a Postdoctoral scientist to join the research group of Dr Edmund Kunji in the MRC Mitochondrial Biology Unit of the University of Cambridge. The postholder will work within a programme focussed on mitochondrial transporters. Transport processes are crucial for the functioning of mitochondria and mutations in transport proteins cause of a wide range of metabolic, neuromuscular and developmental diseases. Basic molecular understanding of their structure and mechanism is required to understand their role in health and disease. The goal of the project is to study their structures in different conformational states by electron cryo-microscopy and/or x-ray crystallography. The post-holder will participate in every stage of the process, from the generation of expression strains or cell lines, isolation of mitochondria, purification and sample preparation, data acquisition and processing, and structure model building and interpretation. There will also be an opportunity to study their role and mechanism using a wide range of biochemical and biophysical techniques. This project is part of a collaborative SNF Sinergia grant together with Profs. Hediger and Lochner of the University of Bern. Candidates will have a PhD in Structural Biology/Biophysics or related disciplines, and a track record of research achievements. Knowledge of protein purification and experience in structural biology are essential. Further details about the job may be found here: http://www.jobs.cam.ac.uk/job/21519/ The MRC Mitochondrial Biology Unit is a world-renowned centre for mitochondrial research. Additional information can be found at www.mrc-mbu.cam.ac.uk. Fixed-term: The funds for this post are available for 3 years in the first instance. The closing date for applications is Wednesday 12th June 2019 with interview date yet to be confirmed. Informal enquiries may be made to Dr Edmund Kunji (ek(a)mrc-mbu.cam.ac.uk).

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Cutting out a fragment from cryoEM map
by Sunandan Mukherjee 14 May '19

14 May '19

Hi, I want to build an RNA model using cryo-EM density. The structure is of a protein-RNA complex and the map consists regions with protein subunits. Is it possible to separate the portion of the map which represents the RNA only? Thanks and regards, Sunandan -- Sunandan Mukherjee (PhD) Research Assistant Laboratory of Bioinformatics and Protein Engineering International Institute of Molecular and Cell Biology (IIMCB) ul. Ks. Trojdena 4, 02-109 Warsaw, Poland

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Low resolution structure determination workshop at ECM32
by Paul Adams 14 May '19

14 May '19

Dear Colleagues, I’d like to draw your attention to a workshop that we’ll be hosting at the 32nd European Crystallographic Meeting in Vienna: Low resolution structure determination and refinement of biological macromolecules by crystallography and cryo-EM Organizers: Paul Adams, Dorothee Liebschner (Lawrence Berkeley Laboratory, Berkeley, USA) Date: 18th August 2019 Time: 9 a.m. – 5 p.m. More details: https://www.ecm2019.org/satellites/ Meeting and satellite registration: https://www.ecm2019.org/submission-registration/registration/online-registr… Cheers, Paul -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley Lab Division Deputy for Biosciences, Advanced Light Source, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Laboratory Research Manager, ENIGMA Science Focus Area Building 33, Room 347 Building 978, Room 4126 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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AUC2019 – early bird registrations closing soon....
by Renwick Dobson 13 May '19

13 May '19

Dear AUC and 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. Registrations are now open and details can be found at this website: https://auc2019.uleth.ca/. Early Bird Registrations close on 15th June. 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>. 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. 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. 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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Electron microscopy software tools workshop at ACA
by Paul Adams 12 May '19

12 May '19

Dear Colleagues, I’d like to draw your attention to a workshop that we’ll be hosting at the American Crystallographic Associate meeting in Covington: Introduction to PHENIX for Electron Cryo-Microscopists Organizers: Paul Adams (Lawrence Berkeley Laboratory, Berkeley, USA) Date: Saturday, July 20, 2019 Time: 9 a.m. – 5 p.m. More details: https://www.aca2019mtg.com/workshops Meeting registration: https://www.aca2019mtg.com/registration Cheers, Paul -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley Lab Division Deputy for Biosciences, Advanced Light Source, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Laboratory Research Manager, ENIGMA Science Focus Area Building 33, Room 347 Building 978, Room 4126 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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MR-Rosetta installation
by Taberman, Helena 09 May '19

09 May '19

Dear Phenix bb, I am facing a problem when trying to instal Rosetta locally. I have installed Rosetta 3.9, set a local environment to my c-shell (setenv PHENIX_ROSETTA_PATH "/Applications/rosetta_src_3.10_bundle") and compiled with ./scons.py -j4 mode=release bin in main/source/ folder. When I try to run rosetta.run_test I get the following error:"OSError: [Errno 2] No such file or directory: '/Applications/rosetta_src_3.10_bundle/main/source/bin' " though the folder is there. Could you please help me? Cheers, Helena -- Helena Taberman, PhD Postdoctoral Researcher Helmholtz-Zentrum Berlin for Materials and Energy Macromolecular Crystallography (HZB-MX) Albert-Einstein-Str. 15 12489 Berlin, Germany Tel: +49 30 8062 14376 Email: helena.taberman(a)helmholtz-berlin.de<mailto:[email protected]> Web: http://www.helmholtz-berlin.de/bessy-mx ________________________________ Helmholtz-Zentrum Berlin für Materialien und Energie GmbH Mitglied der Hermann von Helmholtz-Gemeinschaft Deutscher Forschungszentren e.V. Aufsichtsrat: Vorsitzender Dr. Karl Eugen Huthmacher, stv. Vorsitzende Dr. Jutta Koch-Unterseher Geschäftsführung: Prof. Dr. Bernd Rech (kommissarisch), Thomas Frederking Sitz Berlin, AG Charlottenburg, 89 HRB 5583 Postadresse: Hahn-Meitner-Platz 1 D-14109 Berlin

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Rosetta cannot Rebuild
by Perry, Kay H. 09 May '19

09 May '19

I am having a problem with mr_rosetta where I cannot make it past the rebuild step. I have made fragment files using the old Robetta Server and I am using a hhpred alignment file, but even if I try with a model_already_placed when I reach rebuilding, I get the following error. protocols.looprelax: === protocols.looprelax: === Remodel protocols.looprelax: === ERROR: frag_libs().size() > 0 ERROR:: Exit from: src/protocols/comparative_modeling/LoopRelaxMover.cc line: 47 7 My PHENIX_ROSETTA_PATH is pointed at /share/apps/necat/programs/rosetta3.4 so I believe I am using version 3.4 of rosetta. Kay Perry NE-CAT 9700 S. Cass Ave. Bldg. 436 E007 Argonne, IL 60439 630-252-0692

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Fwd: NIH/NSF-Funded Research Specialist Position in Structural Biology at the University of Illinois at Chicago
by Yury Polikanov 08 May '19

08 May '19

NIH/NSF-Funded Research Specialist Position in Structural Biology at the University of Illinois at Chicago The Polikanov Laboratory at the University of Illinois at Chicago (IL, USA) is looking for talented, skillful, and highly motivated researchers to fill the NIH/NSF-funded Visiting Research Specialist positions to study the structure and function of the bacterial ribosome. The research in the Polikanov Laboratory is focused on understanding the basic principles of protein synthesis in bacteria, the modes of action of ribosome-targeting antibiotics, and the mechanisms of drug resistance at a structural level. More information about Dr. Polikanov research can be obtained from the most recent publications ( https://www.ncbi.nlm.nih.gov/sites/myncbi/yury.polikanov.1/bibliography/503…) or found on the laboratory web-page ( https://bios.uic.edu/bios/people/faculty/yury-polikanov). The successful candidate will be involved in determination of high-resolution structures of ribosome functional complexes with various protein translation factors, tRNAs, and antibiotics using macromolecular X-ray crystallography techniques. Basic qualifications: • BS degree in chemistry, biochemistry, biophysics, or a related field is required; • MS degree or higher is preferred;• Minimum of 3 years of laboratory research experience is required; • Strong background in biochemistry and molecular biology is required; • Practical skills with the most standard methods currently used in molecular biology, and biochemistry (such as protein expression, purification); • Experience in structural biology (cryo-EM or X-ray crystallography) is not required but is highly desirable; • Experience in RNA biology field is not required but is highly desirable; The successful candidate is also expected to: • Act independently in terms of planning and executing the experiments; • Compile, analyze, and prepare data for publications; • Assist with training of graduate and undergraduate students. Interested candidates should submit their CV, cover letter, and contact information for three references at https://jobs.uic.edu/job-board/job-details?jobID=113640&job=visiting-resear… by June 28, 2019. Cover letter should be describing how previous research accomplishments and scientific interests of a candidate fit with the scope of the research in the Polikanov Lab. The University of Illinois at Chicago is an Equal Opportunity, Affirmative Action employer. Minorities, women, veterans and individuals with disabilities are encouraged to apply. The University of Illinois may conduct background checks on all job candidates upon acceptance of a contingent offer. Background checks will be performed in compliance with the Fair Credit Reporting Act *Jacquelyn DeLaurentis* *Human Resource Associate* *Department of Biological Sciences* *The University of Illinois at Chicago* *845 W Taylor St. * *3238 SES, MC 066* *Chicago, IL 60607* *(312) 996-2213 * *jdelaur(a)uic.edu <jdelaur(a)uic.edu>* [image: UIC Logo]

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phenix-1.15.2-3472 crashes with multiple CIF's
by oleg＠quantumbioinc.com 03 May '19

03 May '19

phenix-1.15.2-3472 crashes at the very end of the refinement when multiple CIF's are given at the command line (see below). Please have a look. Thanks Oleg Borbulevych, Ph.D. Staff Scientist QuantumBio, Inc. 2790 W. College Ave. State College, PA 16801 E-mail: oborbulevych(a)yahoo.com, oleg(a)quantumbioinc.com Linkedin Professional Profile: https://www.linkedin.com/in/oleg-borbulevych-b8045422 ============================== Exporting results ============================== Writing refined structure to PDB file: /home/oleg/TEST2/astex/full_set/astex_oniom_qm5_5_01_19/1N2J/1N2J-H_refine_001.pdb n_use = 9639 n_use_u_iso = 9639 n_use_u_aniso = 0 n_grad_site = 0 n_grad_u_iso = 0 n_grad_u_aniso = 0 n_grad_occupancy = 0 n_grad_fp = 0 n_grad_fdp = 0 total number of scatterers = 9639 Writing refined structure to CIF file: /home/oleg/TEST2/astex/full_set/astex_oniom_qm5_5_01_19/1N2J/1N2J-H_refine_001.cif Traceback (most recent call last): File "/home/oleg/phenix-1.15.2-3472/build/../modules/phenix/phenix/command_line/refine.py", line 11, in <module> command_line.run(command_name="phenix.refine", args=sys.argv[1:]) File "/home/oleg/phenix-1.15.2-3472/modules/phenix/phenix/refinement/command_line.py", line 162, in run refine_object.write_model_cif_file(f_cif_model) File "/home/oleg/phenix-1.15.2-3472/modules/phenix/phenix/refinement/driver.py", line 984, in write_model_cif_file additional_blocks=[cif_block]) File "/home/oleg/phenix-1.15.2-3472/modules/cctbx_project/mmtbx/model/model.py", line 964, in model_as_mmcif restraints = self.extract_restraints_as_cif_blocks() File "/home/oleg/phenix-1.15.2-3472/modules/cctbx_project/mmtbx/model/model.py", line 862, in extract_restraints_as_cif_blocks if '_chem_comp_plane_atom.comp_id' in loop.keys(): AttributeError: 'NoneType' object has no attribute 'keys'

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Computational Crystallography Newsletter (CCN) submissions
by Nigel Moriarty 02 May '19

02 May '19

Folks Calling for articles and short communications of interest to structural biologists. The deadline for submission for the July 2019 issue is 20 May 2019. The previous issue is available http://phenix-online.org/newsletter/ and contains the following. January 2019 <http://phenix-online.org/newsletter/CCN_2019_01.pdf> Short Communications - MARCO: The Machine Recognition of Crystallization Outcomes <http://phenix-online.org/newsletter/CCN_2019_01.pdf#page=7> - Building a model the way you do: Map-to-model version 2 <http://phenix-online.org/newsletter/CCN_2019_01.pdf#page=9> Fitting tips #16 – Asn and Gln are remarkably different <http://phenix-online.org/newsletter/CCN_2019_01.pdf#page=1> FAQ - Are the defaults the best for refinements? <http://phenix-online.org/newsletter/CCN_2019_01.pdf#page=6> 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 <https://urldefense.proofpoint.com/v2/url?u=http-3A__www.phenix-2Donline.org…>. Cheers Nigel 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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geometry_restraints.edits.scale_restraints
by Wei Wang 02 May '19

02 May '19

Dear PHENIX developers, I would like to know if the refinement.geometry_restraints.edits.scale_restraints still a valid option for tightening local restraints. I didn’t see this option from the phenix —show-defaults=all. I saw this option on the FAQ webpage. thx Wei

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Phaser Small Molecule MR
by Whitley, Matthew J 02 May '19

02 May '19

Hello all, We have collected electron diffraction data to approximately 1.8 Å on a 'small molecule' of roughly 1660 Da. The space group (P 43 21 2) and unit cell parameters determined during data reduction match the known, published values, and our data are roughly 80% complete in all resolution shells from 17 - 1.8 Å. We would like to solve this structure by molecular replacement in Phaser, but are having a bit of difficulty doing so. Our problems all seem to be related to specifying the composition of the target molecule for Phaser. Via the phenix GUI, we can only specify the target composition as either protein or nucleic acid, when in fact the target is neither. The chemical composition of the target is C72 H85 N19 O18 S5. Is there a way to feed this chemical composition to Phaser and to get it to understand that the target is neither protein nor nucleic acid? Furthermore, according to our reading of the Phaser documentation, specifying "protein" leads to an assumed solvent content of 50%, which is likely to be a substantial overestimation for this small molecule crystal. We have also run into the problem of Phaser complaining that the target molecule will not fit into the given unit cell, which we think is due to the assumption of 50% solvent content. We would be thankful for whatever advice you may have on using Phaser with non-protein, non-nucleic acid molecules. Matthew --- Matthew J. Whitley, Ph.D. Research Instructor W. Furey Lab Department of Pharmacology & Chemical Biology University of Pittsburgh School of Medicine

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Phenix elbow unable to determine bonding
by Ahmad Khalifa 01 May '19

01 May '19

I'm not sure why I'm getting this error. I generated restraint files for GDP with no problems. I noticed that if I change the coordinates of my files, I have to regenerate a new restraint files to match the new coordinates. This time I'm getting this error that I couldn't troubleshoot: Please find attached my gdp.pdb. --------- ['/storage/IJ/.phenix/project_data/elbow_88.eff'] --------- <function run at 0x7fbd2b4bb938> Working parameter elbow { input { chemical_file_name = None chemical_file_name_type = *auto pickle chemical_string = None chemical_string_type = *smiles sequence geometry_file_name = /storage/00_Marina_Ahmad/Tubulin/real_space_refinement/GDP.pdb geometry_file_name_usage = *topology initial orientation final assist template_file_name = None chemical_components_code = None residue = None read_only = False do_all = False optimisation_choice = None *auto am1 mogul ampac gamess gaussian jaguar \ mopac nwchem orca qchem } defaults { id = """GDP""" name = None pH = low *neutral high random_seed = None add_hydrogens = None write_hydrogens = True write_redundant_dihedrals = False multiple_planes = False auto_bond_cutoff = 1.95 pdb_attributes { resseq = 1 icode = None chain_id = A } } optimisation { steps = None tolerence = loose *default tight memory = 1000Mb energy_validation = None third_party_apps { nprocs = 1 method = *uhf mp2 b3lyp basis = *am1 sto-3g 3-21g 6-31g 6-31g(d) 6-31g(d,p) aux_basis = None } } view { view_results = *None reel molden pymol } output { no_output = False output = None output_dir = /storage/00_Marina_Ahmad/Tubulin/real_space_refinement/ pass_through_input_restraints = None pass_through_library_restraints = None output_file_formats = *pdb *cif pdb_ligand tripos sdf data_sheet png xyz \ maestro data_header_file = "" job_title = """GDP""" overwrite = False console_output = *default quiet silent chiral = *retain both enumerate pucker = *random enumerate define pucker_definition = "" cis_trans = *retain enumerate png = False } special { regno = None secondary_smiles = None amgen_id = None } non_user_parameters { opt_type = simple input_type = pdb_rich use_template = False } } ------------------------------------------------------------------------------ electronic Ligand Builder & Optimisation Workbench (eLBOW) 1.14-3260 None - Nigel W. Moriarty (NWMoriarty(a)LBL.Gov) ------------------------------------------------------------------------------ Option opt_type not available Option input_type not available Option job_title not available Option use_template not available Random number seed: 3628800 Initial processing time : 0.00 seconds 0:00 Parsing Parsing Parsing Parsing Parsing Parsing Parsing Parsing Parsing P Input format is PDB MoleculeClass : C:10 N: 5 O:11 P: 2 (PDB format) 28 atoms 30 bonds 0 angles 0 dihedrals 0 rings 0 chirals Predicted memory usage by semi-empirical method : 45Mb Timing estimates Python portion / ATP : 86% c++ optimisation cycle / ATP : 76% 0:00 Bondise Bondise Bondise Bondise Bondise Bondise Bondise Bondise Bondise B Failed to determine the bonding of a fragment of the molecule. PDB file elbow.GDP.GDP_pdb.001.pdb written. Bonding file elbow.GDP.GDP_pdb.001.bonding.py written. Edit bonding file to reflect the desired bond. ALTERNATIVELY Re-run eLBOW with the --reel option and the molecule wil be loaded into REEL. Edit the bonds and save the results as "fixed.cif" to allow eLBOW to load the bonding. You can also use a pull-down menu to push to eLBOW.

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NIH/NSF-Funded Research Specialist Position in Structural Biology at the University of Illinois at Chicago
by Yury Polikanov 01 May '19

01 May '19

NIH/NSF-Funded Research Specialist Position in Structural Biology at the University of Illinois at Chicago The Polikanov Laboratory at the University of Illinois at Chicago (IL, USA) is looking for talented, skillful, and highly motivated researchers to fill the NIH/NSF-funded Visiting Research Specialist positions to study the structure and function of the bacterial ribosome. The research in the Polikanov Laboratory is focused on understanding the basic principles of protein synthesis in bacteria, the modes of action of ribosome-targeting antibiotics, and the mechanisms of drug resistance at a structural level. More information about Dr. Polikanov research can be obtained from the most recent publications ( https://www.ncbi.nlm.nih.gov/sites/myncbi/yury.polikanov.1/bibliography/503…) or found on the laboratory web-page ( https://bios.uic.edu/bios/people/faculty/yury-polikanov). The successful candidate will be involved in determination of high-resolution structures of ribosome functional complexes with various protein translation factors, tRNAs, and antibiotics using macromolecular X-ray crystallography techniques. Basic qualifications: • BS degree in chemistry, biochemistry, biophysics, or a related field is required; • MS degree or higher is preferred;• Minimum of 3 years of laboratory research experience is required; • Strong background in biochemistry and molecular biology is required; • Practical skills with the most standard methods currently used in molecular biology, and biochemistry (such as protein expression, purification); • Experience in structural biology (cryo-EM or X-ray crystallography) is not required but is highly desirable; • Experience in RNA biology field is not required but is highly desirable; The successful candidate is also expected to: • Act independently in terms of planning and executing the experiments; • Compile, analyze, and prepare data for publications; • Assist with training of graduate and undergraduate students. Interested candidates should submit their CV, cover letter, and contact information for three references at https://jobs.uic.edu/job-board/job-details?jobID=113640&job=visiting-resear… by June 28, 2019. Cover letter should be describing how previous research accomplishments and scientific interests of a candidate fit with the scope of the research in the Polikanov Lab. The University of Illinois at Chicago is an Equal Opportunity, Affirmative Action employer. Minorities, women, veterans and individuals with disabilities are encouraged to apply. The University of Illinois may conduct background checks on all job candidates upon acceptance of a contingent offer. Background checks will be performed in compliance with the Fair Credit Reporting Act *Jacquelyn DeLaurentis* *Human Resource Associate* *Department of Biological Sciences* *The University of Illinois at Chicago* *845 W Taylor St. * *3238 SES, MC 066* *Chicago, IL 60607* *(312) 996-2213 * *jdelaur(a)uic.edu <jdelaur(a)uic.edu>* [image: UIC Logo]

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modelling into positive densities
by Sam Tang 30 Apr '19

30 Apr '19

Hello, I am refining a structure solved to 1.5A by MR. Rw/Rf were 0.17/0.22 which seem acceptable to me. At the very beginning part of the protein the electron density is a bit wobbly. I am able to build the residues into the positive densities. But after phenix.refine the chain always shifts away a bit and leaves the green blobs there. (Photo: https://drive.google.com/open?id=1UngAJuEUt1S0LwPybMJLw2E1xA4cNM3R) I am thinking if this can be solved by adjusting the target weights. Or can I apply certain restraints only to those few residues? I refined XYZ (reciprocal space), XYZ (real space), individual B-factors, TLS and occupancies. Thanks in advance. Regards Sam

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molprobity vs validation_cryoem
by Roberto Marabini 28 Apr '19

28 Apr '19

Hi guys, We are using phenix version 1.15.2-3472. We have executed molprobity using the command line: phenix.python_1.15.2-3472 /usr/local/phenix-1.15.2-3472/modules/cctbx_project/mmtbx/command_line/molprobity.py "path_to_pdb"/refmac-refined.pdb pickle=True nproc=4 We have also executed validation_cryoem (here we have used both the GUI and the command line and both interfaces return the same result) phenix.python_1.15.2-3472 ./phenix/phenix/command_line/validation_cryoem.py "path_to_pdb"/refmac-refined.pdb "path_to_map"/molprobity.mrc resolution=3.2 pickle=True What we do not fully understand is why the two commands return different results for molprobity. Are the default parameters different? For example, validation_cryoem reports as number of outliers "34" in the molprobity tab (model.geometry.angle.outliers) while molprobity reports 21 The test files are available at: 3Dmap: https://drive.google.com/open?id=0B_i_LJfUN1z7amoyM1B2N1U0Y2VYODB6LWdLY1pwa… pdb file: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5093775/ Thanks for the help

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weak anomalous phasing (magic triangle I3C)
by ChenTiantian 25 Apr '19

25 Apr '19

Dear all, I'm working on a 18kD protein, the secondary structure prediction says most of the structure is beta sheets, trying to solve the structure with SAD. Heavy atom soaking gives several datasets with I, W, Au, range from 2.7~3.7A, however, the anomalous signal is pretty weak, I couldn't find a reasonable solution. We got a co-crystal dataset with the magic triangle I3C, extends to around 2.5A, this is the best data we got so far. shelxc gives me the following result: Resl. Inf. 12.59 7.75 5.84 4.77 4.08 3.59 3.22 2.94 2.70 2.51 2.35 N(data) 79 257 429 635 811 1010 1235 1384 1698 1555 1954 Chi-sq 0.69 0.63 0.60 0.67 0.61 0.88 1.05 1.02 0.80 0.55 0.42 <I/sig> 79.4 34.1 30.3 32.2 31.8 26.6 21.1 14.6 8.3 3.9 2.4 %Complete 94.0 98.1 97.5 99.5 99.4 99.0 99.7 100.0 99.9 85.4 96.1 Multipl. 4.0 4.5 3.9 4.5 4.7 4.2 4.4 4.8 5.0 4.3 4.4 R(pim)% 2.27 1.72 2.29 2.05 2.02 2.62 3.51 4.84 7.90 14.43 22.78 Ranom% 6.49 3.68 5.19 4.29 4.27 6.35 9.50 12.97 20.90 33.58 52.21 <d"/sig> 0.73 0.80 1.08 0.85 0.95 1.03 1.00 0.91 0.85 0.78 0.70 CC(1/2) 5.1 41.7 68.8 38.1 42.7 49.9 49.9 25.5 24.9 13.3 -4.7 then I tried shelxd with different heavy atom sites number and resolution cut, the best CC I got is CC/CCweak: 24.75/7.69, and I can identify a triangle, (length: 6.5/6.5/5.0A), however, both shelxe and autosol didn't end up with a promising result. [image: image.png] It would be great if anyone can give me some suggestions. Thank you in advance! -- Tiantian

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2 positions around XChem-related compound design
by Frank von Delft 24 Apr '19

24 Apr '19

Dear all, I have two open to work on fragment/XChem-related methodology for structure-based compound design. Team Leader (applications close next *Weds 1st May*): full ad here <https://www.thesgc.org/careers/oxford/sgc-oxford-team-leader-xchem>, summary: /We are recruiting an experienced computational chemist or scientific programmer, to head the Fragalysis project for automating fragment hit progression, part of the XChem collaboration between SGC and Diamond... The //Fragalysis <https://fragalysis.diamond.ac.uk/>//project leader will be tasked with converting the existing proof-of-concept tool into a production-level system that is routinely usable for analysing XChem results and designing and acquiring follow-up compounds. This will entail setting the scientific direction and priorities of the project through close and continuous interaction with expert and novice users; coordinating a growing team of scientific programmers and contractors; liaising with and expanding a wide and international set of collaborators and contributors; securing further funding for the project; helping supervise students; and developing specific methodologies of their own./ Postdoc (closing *Weds 15th May*): full advert here <https://www.thesgc.org/careers/oxford/sgc-oxford-postdoctoral-research-scie…>, this is a summary: /This role will be tasked with the design and acquisition of follow-up compounds based on fragment screening hits from the Target Enabling Package (//www.thesgc.org/tep <http://www.thesgc.org/tep>//) and Ultra-DD (//www.ultra-dd.org <http://www.ultra-dd.org>//) programs. The successful candidate will coordinate experimental validation of the newly designed compounds with collaborating scientists in order to progress them towards potent molecules. / Cheers Frank -- Prof Frank von Delft Associate Professor Principal Investigator: Protein Crystallography Structural Genomics Consortium Oxford University +44 1865 617583 (office: W,F) Principal Beamline Scientist: I04-1 Diamond Light Source +44 1235 778997 (office: M,T,T) +44 7471 026103 (mobile)

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HFIR/SNS Advanced Neutron Diffraction and Scattering Workshop - HANDS 2019
by Meilleur, Flora 22 Apr '19

22 Apr '19

First announcement HANDS 2019 HFIR/SNS Advanced Neutron Diffraction and Scattering Workshop Oak Ridge, TN. June 19 - June 14, 2018 Oak Ridge National Laboratory, in conjunction with North Carolina State University, and support from the National Science Foundation and the Shull Wollan Center - a Joint Institute for Neutron Scattering, celebrates a decade of neutron scattering education in structural biology at ORNL with the HFIR/SNS Advanced Neutron Diffraction and Scattering workshop (HANDS 2019). Detailed information can be found on the workshop web page: https://conference.sns.gov/hands2019/ Application deadline: April 29, 2019 Fellowships to support travel and accommodation are available. No registration fee. The workshop aims at enabling structural biologists to fully exploit the latest instrumentation and software development at the SNS and HFIR facilities at Oak Ridge National Laboratory. Participants of HANDS 2019 will become familiar with neutron techniques with hands-on experiments in sample preparation, crystallography, small angle scattering, reflectometry and neutron spin echo. The workshop is designed for graduate students, post-doctoral fellows and faculty with limited to no experience with neutron sciences. Flora Meilleur, Ph. D Neutron Scattering Scientist, Neutron Scattering Division Oak Ridge National Laboratory Associate Professor, Molecular and Structural Biochemistry North Carolina State University

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Phenix version 1.15 released
by Paul Adams 18 Apr '19

18 Apr '19

The Phenix developers are pleased to announce that version 1.15 of Phenix is now available (build 1.15.2-3472). Binary installers for Linux, Mac OSX, and Windows platforms, and the source installer, are available at the download site: http://phenix-online.org/download/ Highlights for this version: New and improved tools - New algorithm for phenix.map_to_model is faster and builds longer chains - phenix.trace_and_build can build protein into maps at resolutions as low as 4.5 A - phenix.fix_insertions_deletions can build models in places where the map is poor - phenix.refine_ca_model for optimizing C-alpha only models - phenix.comparama for generating Kleywegt-like plots that show how residues moved in the Ramachandran plots before and after refinement - eLBOW can find unique instances of a ligand from the PDB and optionally create Polder OMIT maps - Updated structural library for phenix.structure_search - Updated ligand library for phenix.ligand_identification - Improved reporting of cis-peptides for residues with altloc atoms - Output of mmCIF format files by default by major tools: phenix.refine, phenix.real_space_refine, phenix.pdbtools - Bugfixes in Phaser-2.8.3 Other improvements - Updated mmCIF support (stuct_conn loop, ligand restraints, sequence) - phenix.refine, phenix.real_space_refine, and phenix.pdbtools will also output models in mmCIF format by default - Dependencies are now based on conda packages, which will be more compatible with new operating systems and will improve consistency across all platforms (macOS, linux, Windows) - Bug fixes For a full list of changes see: http://www.phenix-online.org/documentation/CHANGES Please note that this publication should be used to cite use of Phenix: PHENIX: a comprehensive Python-based system for macromolecular structure solution. P. D. Adams, P. V. Afonine, G. Bunkóczi, V. B. Chen, I. W. Davis, N. Echols, J. J. Headd, L.-W. Hung, G. J. Kapral, R. W. Grosse-Kunstleve, A. J. McCoy, N. W. Moriarty, R. Oeffner, R. J. Read, D. C. Richardson, J. S. Richardson, T. C. Terwilliger and P. H. Zwart. Acta Cryst. D66, 213-221 (2010). 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, Lawrence Berkeley Lab Division Deputy for Biosciences, Advanced Light Source, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Laboratory Research Manager, ENIGMA Science Focus Area Building 33, Room 347 Building 978, Room 4126 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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NIH/NSF-Funded Post-Doctoral Positions at the University of Illinois at Chicago (UIC)
by Yury Polikanov 18 Apr '19

18 Apr '19

*NIH/NSF-Funded Post-Doctoral Positions in Structural Biology at the University of Illinois at Chicago (UIC) to Study the Ribosome* [image: Movie_S3_70S-mtRNA_320x240.gif] Prof. Polikanov Laboratory at the University of Illinois at Chicago (IL, USA) is looking for a talented, skillful, and highly motivated researchers to fill the *NIH/NSF-funded Post-Doctoral Scholar *positions to study the structure and function of the bacterial ribosome. The research in the Polikanov Laboratory is focused on understanding the basic principles of protein synthesis in bacteria, the modes of action of ribosome-targeting antibiotics, and the mechanisms of drug resistance at a structural level. More information about Dr. Polikanov research can be obtained from the most recent publications (*https://www.ncbi.nlm.nih.gov/sites/myncbi/yury.polikanov.1/bibliography/50395623/public/?sort=date&direction=descending <https://www.ncbi.nlm.nih.gov/sites/myncbi/yury.polikanov.1/bibliography/503…>*) or found on the web-page ( https://bios.uic.edu/bios/people/faculty/yury-polikanov). The successful candidate will be involved in the determination of high-resolution structures of ribosome functional complexes with various protein translation factors, tRNAs, and antibiotics using macromolecular X-ray crystallography techniques. *Basic qualifications:* - PhD in chemistry, biochemistry , biophysics, or a related field; - Practical skills with the most standard methods currently used in molecular biology, and biochemistry (such as protein expression, purification); - Experience in structural biology (cryo-EM or X-ray crystallography); - Experience in RNA biology field is desired; *The successful candidate is also expected to:* - Drive projects forward; - Act independently in terms of planning and executing the experiments; - Compile, analyze, and prepare data for publications; - Assist with training of graduate and undergraduate students. Review of applications will begin immediately and will continue until the position is filled. Interested candidates should send their CV, cover letter, and contact information for three references directly to Dr. Yury Polikanov at yuryp(a)uic.edu. *Cover letter should be **describing how previous research accomplishments and scientific interest of a candidate fit with the scope of the research in the Polikanov Lab.* -- ------------------------------ Yury Polikanov, Ph.D. Assistant Professor Department of Biological Sciences College of Liberal Arts and Sciences University of Illinois at Chicago 900 South Ashland Avenue, MBRB 4170 Chicago, IL 60607 Tel: 1-312-413-2408 (Office) Tel: 1-312-355-0463 (Laboratory) Fax: 1-312-413-2691 E-mail: yuryp(a)uic.edu Web-Page: *http://bios.uic.edu/bios/people/faculty/yury-polikanov <http://bios.uic.edu/bios/people/faculty/yury-polikanov>* [image: Inline image 1] ------------------------------

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MRage & hhr
by Karolina Michalska 13 Apr '19

13 Apr '19

Hi, I've been trying to run MRage with an hhr file from HHPred, without much success. Phenix claims it does not recognize my hhr file. This is in the latest official release, I've tried older versions with the same outcome. I'll appreciate your help. Karolina

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naive question how to add GTP as a residue to a nucleic acid chain and refine!
by Almudena Ponce Salvatierra 12 Apr '19

12 Apr '19

Dear all, I would like to add a GTP residue to a nucleic acid chain. For so I followed the following steps in coot: add monomer from library, GTP, changed chain ID and residue number accordingly, and then Extensions --> Modelling --> link 2 atoms. I got a dashed line between the 3'O of the GTP and the phosphate of the neighboring nucleotide, and then I used the real space refine tool. Up to here, it all looked promising. In phenix refine I run elbow and readyset and provided cif files, but after phenix.refine I find out that the link between GTP and it's neighbor is gone. How to preserve the bond? Thank you very much in advance!! Best, Almudena

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12th CCP4/APS Crystallographic School in the US
by Xu, Qingping 11 Apr '19

11 Apr '19

Dear Colleagues, We are pleased to announce the 12th annual CCP4 crystallographic school “From data collection to structure refinement and beyond” will be held on June 17-24, 2019 at Advanced Photon Source (APS), Argonne National Laboratory (ANL), near Chicago, Illinois, USA. All details can be found at the school website: http://www.ccp4.ac.uk/schools/APS-2019/index.php. Dates: June 17 through 24, 2019 Location: Advanced Photon Source, Argonne National Laboratory, Argonne (Near Chicago), Illinois, USA The school comprises two parts: data collection workshop and crystallographic computing workshop. Data collection workshop includes beamline training, data collection on GM/CA@APS beamlines 23ID-D and 23ID-B equipped with Pilatus3 6M and Eiger 16M detectors respectively, and data processing. For data collection, only the participants' crystals will be used. Crystallographic computation workshop will feature many modern crystallographic software packages taught by authors and other experts. The daily schedule will be organized in three sections – lectures, tutorials, and hands-on (interactive trouble-shooting of the technical difficulties the participants face in their projects). We have had considerable success resolving these problems in past years, attested by resulting publications (see http://www.ccp4.ac.uk/schools/APS-school/publications.php). A sample program, contact info and other details can be found at the School website. Applicants: Graduate students, postdoctoral researchers and early-career faculty, along with commercial/industrial researchers are encouraged to apply. Only 20 applicants will be selected for participation. Participants of the workshop are strongly encouraged to bring their own problem data sets or crystals so the problems can be addressed during data collection and/or computation workshops. Application: Application deadline is April 15th, 2019. To apply, visit https://www.ccp4.ac.uk/schools/APS-2019/application.php. Fees: The registration for application is free but there is $500 participation fee for the selected academic students and $950 for the industrial researchers. The link for the on-line payments and instructions will be provided once the selection process is completed. The students will be responsible for their transportation and lodging. The workshop organizers can assist in making the lodging reservations at the Argonne Guest House. The workshop will cover all other expenses (including meals). We hope to see you at the school. Charles, Garib and Qingping

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Re: [phenixbb] CryoFit run failure
by Kim, Doo Nam 11 Apr '19

11 Apr '19

Hello Joseph, Sorry for late reply, your email was not in my inbox. I just changed my setting so that email to phenixbb(a)phenix-online.org will come to my inbox directly. Thank you for sharing your input file. I just ran your input pdb file, it appears that "SO4, "CD" are not in amber03 forcefield. I just added my comments like this Solution if these residue/atoms are important: Fix wrong names of atoms/residues. Running real_space_refine via phenix GUI will show which atoms need to be removed/fixed If gromacs amber03 force field doesn't have parameters for these residue/atoms, you may need to add parameters. It is rather a sad fact that most MD simulation force fields do not support all kinds of rare residue/atoms. cryo_fit2 is under development to address this issue using phenix.eLBOW Solution if these residue/atoms are not important: Remove these \"wrong\" atoms/residues from user's input pdb file. Run cryo_fit again Solution if your user's pdb file is big: Probably cryo_fit will change conformation just minimally, I would extract out these \"wrong\" atoms/residues from user's input pdb file, then add these extracted lines to cryo_fitted file If you do git pull at your <phenix>/modules/cryo_fit and run again, you will see results at least to the final stage (that I can't run because of lack of map). best regards, Doonam ________________________________ From: Finney, Joseph (NIH/NCI) [C] <joseph.finney(a)nih.gov> Sent: Monday, April 8, 2019 9:09:23 AM To: Kim, Doo Nam Cc: bugs-from-web(a)phenix-online.org; phenixbb(a)phenix-online.org; Esser, Lothar (NCI) Subject: CryoFit run failure Hey Doonam, As I said before I figured I would have some additional questions. The new version of phenix (1.15-3459-000) fixed my issues last week with the tutorial dataset. However, I am having trouble with our own testing dataset. As before we are testing in GUI version first. I am using the same run conditions for both the tutorial set and out testing set. I am attaching the log of the tutorial set as well as the log of our testing set and the test PDB. The density map is too large for email. The major error I see is “Step 1 didn't run successfully” from the ferrtest run. Looking at the tutorial PDB, it seems as though the header, the terminations, and the nonstandard atoms have been removed prior to use. I tried this and got a different error: “pdb file cleaning is not done, exit now” Do you have any recommendations on how to succeed? Thanks in advance! Joseph Finney [Contractor] Software Developer National Cryo-EM Facility Cancer Research Technology Program Frederick National Laboratory for Cancer Research Leidos Biomedical Research Inc. PO Box B Frederick, MD 21702 Tel: (301) 228-4313 Cell: (615) 512-2053 Joseph.finney(a)nih.gov<mailto:[email protected]>

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Faculty equivalent cryoEM position
by Hasan, Syed Saif 11 Apr '19

11 Apr '19

************************************************************************************************** Faculty-Equivalent, Cryo-Electron Microscopy (Cryo-EM) Position Summary: As part of its program focused on advancing new measurement technologies and standards for biomolecular structure and function, the National Institute for Standards and Technology (NIST) Biomolecular Structure & Function Group seeks a ‘faculty-equivalent’ principle investigator to establish a research program focused on applications of cryo-electron microscopy (cryo-EM) in structural biology. We are particularly interested in candidates with a focus on developing cryo-EM experimental techniques and data analysis tools, and who would leverage other structure methods [e.g. nuclear magnetic resonance (NMR), macromolecular crystallography and/or small angle scattering], to advance the current state-of-the-art in structure-function analysis of biological systems of biopharmaceutical interest. The successful candidate should have a PhD or equivalent, a strong research portfolio and publication record that demonstrates evidence of cryo-EM expertise complementary to current group research strengths in NMR, crystallography and small angle scattering. He/she is expected to become a recognized leader in the field of cryo-EM and contribute to collaborative projects both within the group and with external partners. US Citizenship is required. The Biomolecular Structure & Function Group is located at the Institute for Bioscience and Biotechnology Research (IBBR<http://www.ibbr.umd.edu/>), a joint federal-state research partnership between NIST and the University of Maryland. IBBR operates state-of-the-art research facilities and is located in the heart of the biotechnology corridor in Rockville, Maryland. The Biomolecular Structure & Function Group is affiliated with the NIST Center for Neutron Research (NCNR<https://www.nist.gov/ncnr>) and the NIST Biomanufacturing<https://www.nist.gov/programs-projects/biomanufacturing-initiative> program. Our cryo-EM facility located at IBBR includes a newly installed 200 kV Talos-Arctica equipped with a Falcon III direct electron detector. A K3 direct electron detector and a Volta phase plate will be acquired soon in addition to a 200 kV Glacios microscope. State-of-the-art computational resources are available through the IBBR High Performance Computing Cluster. Salary: Commensurate with qualifications. Applications: Applicants should send cover letter, curriculum vitae, research statement, and contact information of three references to the attention of John P. Marino, Leader, Biomolecular Structure & Function Group: john.marino(a)nist.gov. ************************************************************************************************** S. Saif Hasan, PhD Assistant Professor Department of Biochemistry and Molecular Biology University of Maryland School of Medicine 108 N. Greene St., Baltimore, MD 21201 Group Leader Center for Biomolecular Therapeutics (CBT) Institute for Bioscience and Biotechnology Research (IBBR) 9600 Gudelsky Drive, Rockville, MD 20850 Phone: 240-314-6396 https://www.ibbr.umd.edu/profiles/s-saif-hasan

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running phenix.validation from command line
by Roberto Marabini 09 Apr '19

09 Apr '19

Hi, I see that it is possible to execute phenix.validation from command line by typing: phenix.validation_cryoem <path to>/5ni1.cif <path to>/molprobity.mrc resolution=2.2 The program runs smoothly and prints on screen a few hundreds of lines. The more or less equivalent program in version 1.13 was phenix.molprobity, when executed with the option pickle=True, phenix.molprobity saved to the hard-disk a pkl file containing all data. Is there an equivalent flag for phenix.validation_cryoem? where is the result of executing this shell being saved? thanks Roberto

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Clashscore and average B
by Sam Tang 08 Apr '19

08 Apr '19

Hello. I am refining a structure with Phenix.refine and encounter an issue which I appreciate your comments. The structure is in P1 and refined to 36A-3A. Rw/Rf = 23.9%/29.1%, RMS bonds 0.002, RMS angles 0.544, Ramachandran favoured 97.5%. The statistics is acceptable to me but two numbers raised my concern. First is the clashscore of 7.7, which is below minimum of other structures shown by Polygon. Second is an average B of 37, with a minimum of 9.2. When I checked again in Coot (Average Temp fact. analysis), none of the residues or water look abnormal. I refined both individual and group B-factors and applied 'Optimize X-ray/adp weight'. So my questions are: (1) if a clashscore too high means a lot of bad contacts, how do you comprehend a clashscore too low? How can I modify my strategy to get around? (2) is there an acceptable low value of B? (I sort of went through a similar thread in phenixbb appeared 9 years ago but seems the discussion did not come to a conclusion). Any advice I should reliax or tighten the adp restraints? PS - it may be worth mentioning the structure contains a OMU nucleotide. The .cif file I used was generated by elbow. The nucleotide looks normal in coot w.r.t. contact or B-value. Thanks a lot! Sam

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X-Ray Methods in Structural Biology @CSHL
by Paul Adams 05 Apr '19

05 Apr '19

Dear All, The June 15th deadline for applications to the CSHL X-ray Methods in Structural Biology Course to be held later this year, October 15 through October 30, 2019 is rapidly approaching. The official course announcement is here: https://meetings.cshl.edu/courses.aspx?course=C-CRYS&year=19 so please pass this on to folks who might be interested and who would benefit. The course is designed for researchers who are either new to, or who wish to increase their in-depth knowledge of, macromolecular crystallography. This immersive course is an outstanding place to learn both the theoretical and practical aspects of Macromolecular Crystallography because of the extensive lectures from world-renowned teachers, which are combined with hands-on experiments. This 2019 course will be lead by Jim Pflugrath (Rigaku, ret.), Tassos Perrakis (NKI), Paul Adams (LBL), Janet Newman (CSIRO) and an All-Star cast of lecturers. Attendees can expect to participate in a course that is unparalleled in the world, with experts each devoting several days to teaching the fundamentals, theory and practical considerations of crystallographic structure solution. We expect to have the participants crystallize several proteins and determine their structures all in about two weeks.Students may also work on their own projects, but not exclusively. They will also become well-versed in the theory of X-diffraction and crystal structure determination while having lots of fun, but not much sleep. There will be a trip to the state-of-the-art beamlines at NSLS-II to collect data. The course is limited to 16 participants due to the very hands-on nature of the experiments and the intimate seminar room and laboratory settings. Please check the above web link for more details. In particular, please note the information about fellowships, scholarships, and stipends that are available. It is often possible for applicants to receive some level of support to help offset the course fee. This course is supported with funds provided by the National Institute of General Medical Sciences for which we are extremely grateful. Also there are stipends available from the Leona M. and Harry B. Helmsley Charitable Trust and the Howard Hughes Medical Institute to help offset the cost of tuition. If anyone has any questions, please send me e-mail, I will be happy to answer any queries. Thanks for spreading the word, Janet, Tassos, Paul, and Jim -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley Lab Division Deputy for Biosciences, Advanced Light Source, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Laboratory Research Manager, ENIGMA Science Focus Area Building 33, Room 347 Building 978, Room 4126 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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column labels for autobuild
by wtempel 04 Apr '19

04 Apr '19

Hi all,how does one specify column labels in a definition file for phenix.autobuild? input_files { map_file_is_density_modified = True input_map_labels = “F PHIDM FOMDM” input_refinement_labels = “F SIGF FreeR_flag” } gives this error: Sorry: Sorry, the label 'F SIGF FreeR_flag' does not exist (or all data is zero) … ...available labels are: ['FreeR_flag', 'F', 'SIGF', 'FC', 'PHIC', 'FC_ALL', 'PHIC_ALL', 'FWT', 'PHWT', 'DELFWT', 'PHDELWT', 'FOM', 'FC_ALL_LS', 'PHIC_ALL_LS', 'PHIDM', 'FOMDM', 'FDM', 'None'] Many thanks in advance. Wolfram Tempel

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Re: [phenixbb] Phenix elbow taxol
by r.joosten＠nki.nl 04 Apr '19

04 Apr '19

Before you make restraints yourself, check whether it is already in the dictionary. The name should be TA1 (http://ligand-expo.rcsb.org/reports/T/TA1/index.html). Cheers, Robbie On 31 Mar 2019 10:45, Georg Mlynek <georg.mlynek(a)univie.ac.at> wrote: Dear Ahmad, one way is to use the smiles string. If taxol if also named Paclitaxel then here it is: https://pubchem.ncbi.nlm.nih.gov/compound/paclitaxel#section=Canonical-SMIL… Then just watch this video on phenix.elbow https://www.youtube.com/watch?v=8qVYTUVKlbQ Br, Georg. On 31.03.19 08:08, Ahmad Khalifa wrote: How can I generate restraint files for taxol? I attached my taxol.pdb for reference. Thanks. _______________________________________________ phenixbb mailing list phenixbb(a)phenix-online.org<mailto:[email protected]> http://phenix-online.org/mailman/listinfo/phenixbb Unsubscribe: phenixbb-leave(a)phenix-online.org<mailto:[email protected]>

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Tantalum cluster
by Alexandra Deaconescu 02 Apr '19

02 Apr '19

Hello, I am trying to phase off Tantalum clusters. According to the Phenix documentation online, one should use TX as a scatter in Hyss. However, this does not work and Phenix complains about "unknown scatter type." Any ideas how to solve this? Thank you, Alexandra -- Alexandra Deaconescu, B.E., Ph.D. Assistant Professor Brown University Office: (401) 863-3215 Wet Lab: (401) 863-6729 Computational Lab: (401) 863-7031

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validation_cryoem
by Daniel Larsson 01 Apr '19

01 Apr '19

Hi, When I use the phenix.validation_cryoem command line tool, I get very little data compared to when I run the Cryo-EM validation from the GUI. Which options should I enable to get things like detailed clash annoation, CaBLAM analysis etc? 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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Phenix elbow taxol
by Ahmad Khalifa 31 Mar '19

31 Mar '19

How can I generate restraint files for taxol? I attached my taxol.pdb for reference. Thanks.

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Call reminder: XChem fragment screening, NEXT WEDNESDAY
by Frank von Delft 29 Mar '19

29 Mar '19

Dear aspiring drug discoverers A reminder that the deadline for the next round of proposals for XChem fragment screening is *next Wednesday 5pm*, as part of Diamond's general Call for Proposals. Full details <https://www.diamond.ac.uk/Instruments/Mx/Fragment-Screening/Applying-for-XC…> are on the XChem webpage <https://www.diamond.ac.uk/Instruments/Mx/Fragment-Screening.html>. *Reminder: *we are now inviting a broader set of projects: * Two-tiered access: if you have an exciting system but don't yet know how to progress it, you can ask for exploratory access ("Tier 1") * BAG access: several labs and collaborations have requested increased flexibility, and several have been assigned Block Allocation Groups. If you wish to submit this route, I suggest you also email me directly. Happy screening! Frank -- Prof Frank von Delft Associate Professor Principal Investigator: Protein Crystallography Structural Genomics Consortium Oxford University +44 1865 617583 (office: W,F) Principal Beamline Scientist: I04-1 Diamond Light Source +44 1235 778997 (office: M,T,T) +44 7471 026103 (mobile)

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scattering_table in phenix.real_space_refine
by Keitaro Yamashita 25 Mar '19

25 Mar '19

Dear PHENIX developers, For the refinement of CryoEM structure, I changed scattering_table to electron from default (n_gaussian in phenix-1.13), but the resultant coordinates and ADPs were exactly same while map-model CCs were improved. Looking into the code, I noticed scattering_table is not passed to the ADP refinement code (mmtbx.refinement.real_space.adp.real_space_group_adp_refinery_via_reciprocal_space) and xray_structure is newly constructed from a pdb_hierarchy object; therefore a default table in scattering_type_registry() (which is n_gaussian) is always used. Is this an intended behavior? I modified the code to use the scattering table of electron in ADP refinement, and CCs were improved (CC_mask 0.7566 to 0.7813; both evaluated with scattering_table=electron). Best regards, Keitaro

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Refinement
by StrBio 24 Mar '19

24 Mar '19

ALL. I have data at 2.4 A in P21 sp gr, helical protein. Refined to Rwork 29 Rfree 34 with nice density map and all nice statistics oither Rfactor (by Phenix). Refmac quit same. Should I deposit it or look better data? Any suggestion?

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Phenix Rosetta hybrid refinement PHENIX_ROSETTA_PATH error
by Ahmad Khalifa 23 Mar '19

23 Mar '19

But I have the path set! (base) [labusr@luxor ~]$ echo $PHENIX_ROSETTA_PATH /home/labusr/rosetta:/home/labusr/rosetta/main I attached the log. Please advise.

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Distance constraint to atom in symmetry copy in phenix.refine
by Julian Esselborn 23 Mar '19

23 Mar '19

Dear community, we have a somewhat complicated problem to which I don't seem to find a solution. We have a structure, which has a number of 3-fold and 2-fold symmetry axes in the final assembly structure. The 3-fold axes are hold together by metal atoms on the axis. However, we have three cases of these axes: 1. Symmetry axis falls onto the crystallographic symmetry axis. We can deal with this; setting metal to 0.33 occupancy and setting metal-protein distance constraints. This is a proper symmetry axis. 2. Symmetry axis doesn't fall onto a crystallographic symmetry axis, but all three monomers coming together are within the same symmetry copy of the ASU. Even easier, metal stays at occ=1 and we just set constraints to chain A, chain B, chain C. 3. The really challenging case, where the axis doesn't fall onto the symmetry axis, but the three monomers coming together are in different symmetry copies of the ASU. Cases (2) and (3) are pseudo-symmetric in the crystallographic sense. Usually a bit of intelligent moving around of the monomers to their crystallographic symmetry positions should push all monomers of case (3) into neighboring positions within the same ASU ending up as case (2); problem solved. BUT: In our structure we have too many 3fold axes, such that there will always be one of them ending up as case (3). E.g. the three monomers are chains A, B, C, but they do not end up neighboring in the ASU. Rather the axis is formed by A, B' and C'' (with ' denoting different symmetry copies of the ASU). We could assign the metal to chain A with occ=1 and no metal in B and C. However, we would need to set a distance constraint from the metal to it's ligands in protein monomer B and protein monomer C. But it is only the ligand in B' and C'', which are actually close to the metal in A. The ligands in B and C are at the other end of the ASU. Is there a way to set a distance constraint such that it measures the distance to a crystallographic symmetry copy? A different idea was to just assign an alternative position alt A, alt B and alt C to the metal, with A being close to the ligand in monomer A, B close to monomer B and C close to monomer C. That way we could make constraints. But we would need to cross fingers that the three metal atoms actually end up in the same spot once applying the crystallographic symmetry (and remember, that 3-fold axis is not constructed by applying a 3fold rotational symmetry around that axis; rather an actual crystallographic symmetry somwhere else brings them together; means the ligands with their metal atoms can actually move independently). I'm a bit at a loss how to deal with this and would appreciate input. Thanks a lot in advance! all the best Julian ---- Julian Esselborn Postdoctoral Researcher Tezcan group University of California, San Diego

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Map Segmantation
by Yangqi Gu 22 Mar '19

22 Mar '19

Hi Everyone, I have a naive question about segmentation. I have a low resolution map of a filament (~20 A) and I know the helical symmetry. I have monomer sequence but no structure. I am wondering if I could segment the filament and obtain the monomer density? Does segment_and_split_map work on the low resolution case? Best, Yangqi -- Yangqi Gu Graduate Student Malvankar Lab Yale University, West Campus

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How to get command line of operation run through gui?
by Ahmad Khalifa 20 Mar '19

20 Mar '19

I'm trying to box out a cryo-em map and used the option "padding=" as per the documentation, but received error interpreting command line argument. is the documentation outdated? Regards.

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mmCIF for deposition
by Patrick Loll 19 Mar '19

19 Mar '19

Hi all, Following the instructions given here: https://www.phenix-online.org/documentation/overviews/xray-structure-deposi… I’m attempting to use mmtbx.prepare_pdb_deposition to insert sequence information into the mmCIF that contains the model coordinates. Unfortunately, the program fails with an error (shown below). The sequence file is FASTA format, and contains an entry for each of the (4) chains in the AU, i.e. >A MSEQNCE… >B MSEQNCE… etc. Any bright ideas? ============this is what happens (vide infra)==================================== [PJL-iMac:blahblah/PJL_final] loll% mmtbx.prepare_pdb_deposition filename.cif seq_name.fasta Starting mmtbx.prepare_pdb_deposition on Mon Oct 1 11:16:23 2018 by loll =============================================================================== Processing files: ------------------------------------------------------------------------------- Found model, filename.cif Found sequence, seq_name.fasta Processing PHIL parameters: ------------------------------------------------------------------------------- No PHIL parameters found Final processed PHIL parameters: ------------------------------------------------------------------------------- data_manager { model { file = “filename.cif" } default_model = “filename.cif" sequence_files = "seq_name.fasta" default_sequence = "seq_name.fasta" } Starting job =============================================================================== Validating inputs Using model: filename.cif Using sequence: seq_name.fasta Creating mmCIF block for sequence Traceback (most recent call last): File "/Applications/phenix-1.14-3260/build/../modules/cctbx_project/mmtbx/command_line/prepare_pdb_deposition.py", line 9, in <module> run_program(program_class=prepare_pdb_deposition.Program) File "/Applications/phenix-1.14-3260/modules/cctbx_project/iotbx/cli_parser.py", line 71, in run_program task.run() File "/Applications/phenix-1.14-3260/modules/cctbx_project/mmtbx/programs/prepare_pdb_deposition.py", line 98, in run alignment_params=self.params.mmtbx.validation.sequence.sequence_alignment) File "/Applications/phenix-1.14-3260/modules/cctbx_project/iotbx/pdb/hierarchy.py", line 1190, in as_cif_block_with_sequence assert len(chain.residue_groups) + chain.n_missing_start + chain.n_missing_end == len(sequence) AssertionError (gouts of smoke, terrified squealing) The ‘No PHIL parameters found’ message is concerning, but the program clearly seems to be finding the input file names. Suggestions welcome. Thanks, Pat --------------------------------------------------------------------------------------- Patrick J. Loll, Ph. D. Professor of Biochemistry & Molecular Biology Drexel University College of Medicine Room 10-102 New College Building 245 N. 15th St., Mailstop 497 Philadelphia, PA 19102-1192 USA (215) 762-7706 pjloll(a)gmail.com pjl28(a)drexel.edu

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FEM by using FoFc map
by Danilo Belviso 18 Mar '19

18 Mar '19

Dear all, I am interested in fitting a ligand in the case of a structure where water molecules have been already placed. I know that this is not the standard procedure, but these water molecules are quite sure. To do this, I used ligand fit procedure with command "lig_map_type = *fo-fc_difference_map fobs_map pre_calculated_map_coeffs" command. At the end, the procedure provides ligands with low CC (0.4-0.55). So, I would try ligand fitting by using FEM of Fo-Fc. The rationale is that FEM of Fo-Fc could help (likely) ligand fitting, by consider the presence of water molecules at the same time (Fo-Fc should be 0 where water molecules are placed). Maybe nothing will change, but I would try. I calculated FEM by using phenix.fem start_FEM.pdb start_FEM.mtz input.xray_data.label='FOFCWT' and also by using phenix.fem start_FEM.pdb start_FEM.mtz maps.map_coefficients_label='FOFCWT PHFOFCWT' file_name_prefix='FEM_map' where start_FEM.pdb and start_FEM.mtz are the pdb and mtz resulting from the refinement with water. However, by checking the the fem maps by coot, I notice that fem is completely different from Fo-Fc and it is not the expected feature-enanched Fo-Fc. Is the procedure and keywords correct to perform FEM calculation of Fo-Fc? Do you have any suggestions? Thanks Danilo -- Dr. Belviso Benny Danilo, PhD Istituto di Cristallografia (IC) Consiglio Nazionale delle Ricerche (CNR) via Amendola 122/o, 70126 Bari - Italy Tel ++39 080 5929273 Fax ++39 080 5929170 mail: danilo.belviso(a)ic.cnr.it web: users.ba.cnr.it/ic/crisdb00

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UK Open Research Data Task Force weblink to Report, Case studies and Minister’s response
by John R Helliwell 18 Mar '19

18 Mar '19

Dear Colleagues, Thankyou for asking about the weblink to the case studies. The UK Open Research Data Task Force weblink to Report, Case studies and Minister’s response is here:- https://www.gov.uk/government/publications/open-research-data-task-force-fi… Best wishes, John

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