January 2021 - phenixbb - phenix-online.org

RapiData 2020 applications open
by Smith, Clyde 16 Nov '21

16 Nov '21

Applications are now open for the 2020 edition of RapiData at SSRL. RapiData is a practical course in macromolecular X-ray diffraction data collection, data processing and structure solution. The aim of the RapiData course is to educate and train young scientists in data collection and processing methods at synchrotron beamlines, using state-of-the-art software and instrumentation. The course will be held in sunny California at the Stanford Synchrotron Radiation Lightsource (SSRL) located on the SLAC National Accelerator Laboratory campus in Menlo Park, CA, from March 30 - April 4 2020. Course organizers for 2020 are Silvia Russi, Clyde Smith and Jeney Wierman. The course will comprise hands-on experiments at the SSRL beamlines, software tutorials, and lectures on the following topics: Specimen preparation, Data collection strategies, X-ray light sources, X-ray detectors, Data reduction, Structure solution by MAD, SAD and Molecular Replacement, Complementary methods (spectroscopy and small angle scattering). Please visit http://smb.slac.stanford.edu/news/rapidata/rapidata-2020/ and use the links on the "registration" page to apply for the course. The application deadline is November 10 2019. Successful applicants will be notified shortly thereafter, and invited to register and book accommodation at the SLAC Guesthouse at that time. A limited amount of travel support funding may be available. Please direct questions to Silvia Russi (srussi(a)slac.stanford.edu), Jeney Wierman (jwierman(a)slac.stanford.edu) or Clyde Smith (csmith(a)slac.stanford.edu).

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Open-rank, tenure-line faculty position
by Hasan, Syed Saif 05 Feb '21

05 Feb '21

Dear Colleagues, The Institute for Bioscience & Biotechnology Research (IBBR) and the University of Maryland, College Park Department of Chemistry & Biochemistry invite applications for an open-rank, tenure-line faculty position in structural biology, with an emphasis in the area of biomolecular cryo-electron microscopy (cryoEM), starting August 2021. The faculty member will base their research program on the IBBR campus in Rockville, Maryland, and hold joint appointments with IBBR and the Department of Chemistry & Biochemistry at College Park. The criteria for selection will be proven excellence and potential for impact through original research, scholarship, and teaching. Successful candidates will be expected to develop a vigorous externally funded research program and have a demonstrated commitment to teaching and mentorship at the undergraduate and graduate levels. IBBR is a joint research institute of the University of Maryland and the National Institute of Standards and Technology (NIST), centrally located in Maryland’s biotechnology corridor. The Institute’s mission is to conduct groundbreaking research in the field of biotechnology that generates innovative solutions to major scientific and engineering challenges. The Institute has a long history of excellence in biomolecular structure-function relationships. Current research programs center on the biomolecular engineering of vaccines, biotherapeutics, and diagnostics; biomolecular measurement science; and disease pathways and biomolecular targets. The available instrumentation at IBBR includes a 200 kV Talos Arctica cryoEM with a Falcon 3EC direct electron detector and a 200 kV Glacios cryoEM with a Gatan K3 direct electron detector and a Volta phase plate. The University of Maryland College Park has a Zeiss EM 10 CA TEM equipped with a tilt stage and a JEOL 100CX II TEM. IBBR instrumentation for sample preparation was recently upgraded with a Thermo Fisher Scientific Vitrobot Mark IV and a Gatan cryoplunge 3. IBBR also maintains a high-performance computing cluster with a dedicated 750 TB parallel file system, and two dedicated 8-GPU nodes. These cryo-EM facilities complement other state-of-the-art instrumentation and expertise at IBBR, including NMR, X-ray crystallography, mass spectrometry, and solution X-ray scattering. For details, please see this advertisement: https://ejobs.umd.edu/postings/80583 Best wishes, Saif S. Saif Hasan, PhD Assistant Professor Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine 108 N. Greene Street, Baltimore MD 21201 https://www.medschool.umaryland.edu/profiles/Hasan-S-Saif-Hasan-Syed-Saif/ Associate Member Program in Oncology, University of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center (UMGCCC) 22 S. Greene Street, Baltimore MD 21201 Office and Laboratory Address: Center for Biomolecular Therapeutics, Institute for Bioscience and Biotechnology Research (IBBR) 9600 Gudelsky Drive, Rockville MD 20850 https://www.ibbr.umd.edu/profiles/s-saif-hasan Phone: 240-314-6396 Fax: 240-314-6225

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Re: [phenixbb] refinement with translational ncs
by Jorge Iulek 31 Jan '21

31 Jan '21

Dear Esko, Thank you for your input. I must also look into these papers. Jorge On 1/27/21 10:02 AM, Esko Oksanen wrote: > Dear Jorge, > > With significant translational pseudosymmetry, at least close to a > pseudo-centerering vector, will inevitably lead to higher R-values. > Basically the R-value isn’t a very good indicator of the structure > correctness any more and the expected values for an acentric structure > are no longer really valid. I had a somewhat similar case long ago > (https://doi.org/10.1107/S0907444906031519) and since then there is a > nice paper summarising the effects of pseudosymmetry > (https://doi.org/10.1107/S090744490705531X). > > HTH, > Esko > *_____________________* > * > * > *Esko Oksanen, PhD* > Instrument Scientist - Neutron Macromolecular Crystallography > > European Spallation Source ERIC > P.O Box 176, SE-221 00 Lund, Sweden > Visiting address: Odarslövsvägen 113 224 84 Lund Sweden > Switchboard: +46 46 888 00 00 > Phone: +46 721 79 20 36 > E-mail: esko.oksanen(a)ess.eu <mailto:[email protected]> > > www.ess.eu <http://www.esss.se/> > > > > > > > > >> On 27 Jan 2021, at 11:46, Jorge Iulek <iulek(a)uepg.br >> <mailto:[email protected]>> wrote: >> >> Dear all, >> >> >> I have a dataset at 2.98 A resolution, images processed to CC_1/2 >> at circa 50% in the last resolution shell, tetramer in the asymmetric >> unit, local (rotational) symmetry 222. Xtriage indicates a peak in >> the Patterson function at 20% height of origin peak, at fractional >> coordinates of 0.0000 0.0000 0.3177. Space group is P21. >> >> I am aware that this brings problems to refinement , as even >> stated at xtriage output "Translational pseudo-symmetry is very >> likely present in these data. Be aware that this will change the >> intensity statistics and may impact subsequent analyses, and in >> practice may lead to higher R-factors in refinement.", and so I can't >> lower my R and R-free below ~31 and 36 % , respectively. >> >> At phenix.refine, setting "tncs_correction = True" brings little >> benefit (what does this actually do? points to references are >> welcome). I wonder nevertheless if some strategy might help in on >> lowering these R's and, of course, allow me to build a better model >> (in spite of the resolution). I tried some combinations of other >> types of ncs and tls groups, with little success. Particularly, it >> seems that the refinement of ADPs are a kind of unstable (what I >> would understand come from the - partial - modular nature of the >> intensities - due to tncs - and these - ADP - would be reflected by >> the intensity fall-off with resolution). What about refining ADPs >> only to a zone which is not affect by data modulation? How to do >> that? Any other ideas? >> >> Thanks, >> >> >> Jorge >> >> >> >> >> _______________________________________________ >> 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 >

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refinement with translational ncs
by Jorge Iulek 31 Jan '21

31 Jan '21

Dear all, I have a dataset at 2.98 A resolution, images processed to CC_1/2 at circa 50% in the last resolution shell, tetramer in the asymmetric unit, local (rotational) symmetry 222. Xtriage indicates a peak in the Patterson function at 20% height of origin peak, at fractional coordinates of 0.0000 0.0000 0.3177. Space group is P21. I am aware that this brings problems to refinement , as even stated at xtriage output "Translational pseudo-symmetry is very likely present in these data. Be aware that this will change the intensity statistics and may impact subsequent analyses, and in practice may lead to higher R-factors in refinement.", and so I can't lower my R and R-free below ~31 and 36 % , respectively. At phenix.refine, setting "tncs_correction = True" brings little benefit (what does this actually do? points to references are welcome). I wonder nevertheless if some strategy might help in on lowering these R's and, of course, allow me to build a better model (in spite of the resolution). I tried some combinations of other types of ncs and tls groups, with little success. Particularly, it seems that the refinement of ADPs are a kind of unstable (what I would understand come from the - partial - modular nature of the intensities - due to tncs - and these - ADP - would be reflected by the intensity fall-off with resolution). What about refining ADPs only to a zone which is not affect by data modulation? How to do that? Any other ideas? Thanks, Jorge

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Postdoctoral Fellow Position in CFTR biology at AbbVie
by Jain, Rinku 26 Jan '21

26 Jan '21

Hello Everyone, A postdoctoral position is available immediately in the Cystic Fibrosis Group led by Dr. Ashvani Singh at AbbVie Inc, in Illinois, USA. Successful candidate will work with a cross-functional team of researchers to Investigate the Structure-Function Relationship of CFTR Using CFTR Modulators and Understand their Clinical Translation. Qualified candidate should have a PhD in Biochemistry (Biochemistry/Pharmacology/Cell and Molecular Sciences/Structural Biology) with no more than 3 years of prior postdoctoral experience. Experience in membrane protein expression, purification and biochemistry is required and a strong background in CFTR pharmacology is preferred. Key responsibilities include expression and purification of disease mutants and biochemical, biophysical, and structural studies. Previous experience in Cryo-EM is preferred but not essential. Selected candidate will have the opportunity to learn Cryo-EM. For more information and to apply online, please visit: https://careers.abbvie.com/jobs/2007216?lang=en-us#.X48n8qJQthg.mailto Req ID: 2100410 Thanks, Rinku

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Phenix version 1.19.1 released
by Paul Adams 25 Jan '21

25 Jan '21

The Phenix developers are pleased to announce that version 1.19.1 of Phenix is now available (build 1.19.1-4122). This fixes bugs in the 1.19 release. If you have previously downloaded 1.19 we recommend upgrading to 1.19.1. 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 the 1.19.1 version of Phenix: - phenix.real_space_refine - Fix bug in restoring previous jobs - Clarify NCS options Please note that this new publication should be used to cite the use of Phenix: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Liebschner D, Afonine PV, Baker ML, Bunkóczi G, Chen VB, Croll TI, Hintze B, Hung LW, Jain S, McCoy AJ, Moriarty NW, Oeffner RD, Poon BK, Prisant MG, Read RJ, Richardson JS, Richardson DC, Sammito MD, Sobolev OV, Stockwell DH, Terwilliger TC, Urzhumtsev AG, Videau LL, Williams CJ, Adams PD: Acta Cryst. (2019). D75, 861-877. https://doi.org/10.1107/S2059798319011471 Full documentation is available here: http://www.phenix-online.org/documentation/ There is a Phenix bulletin board: http://www.phenix-online.org/mailman/listinfo/phenixbb/ Please consult the installer README file or online documentation for installation instructions. Direct questions and problem reports to the bulletin board or: help(a)phenix-online.org and bugs(a)phenix-online.org Commercial users interested in obtaining access to Phenix should visit the Phenix website for information about the Phenix Industrial Consortium. The development of Phenix is principally funded by the National Institute of General Medical Sciences (NIH) under grant P01-GM063210. We also acknowledge the generous support of the members of the Phenix Industrial Consortium. -- Paul Adams Division Director, Molecular Biophysics & Integrated Bioimaging, LBL (http://biosciences.lbl.gov/divisions/mbib) Principal Investigator, Computational Crystallography Initiative, LBL (http://cci.lbl.gov) Vice President for Technology, the Joint BioEnergy Institute (http://www.jbei.org) Principal Investigator, ALS-ENABLE, Advanced Light Source (http://als-enable.lbl.gov) Division Deputy for Biosciences, Advanced Light Source (https://als.lbl.gov) Laboratory Research Manager, ENIGMA Science Focus Area (http://enigma.lbl.gov) Adjunct Professor, Department of Bioengineering, U.C. Berkeley (http://bioeng.berkeley.edu) Adjunct Professor, Comparative Biochemistry, U.C. Berkeley (http://compbiochem.berkeley.edu) Building 33, Room 250 Building 978, Room 4126 Building 977, Room 180C Tel: 1-510-486-4225 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 33R0345 Berkeley, CA 94720, USA. Executive Assistant: Ashley Dawn [ ashleydawn(a)lbl.gov ][ 1-510-486-5455 ] --

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real space rotamer restrains
by Leonid Sazanov 22 Jan '21

22 Jan '21

Hi, Is there somewhere a description of all the new parameters in phenix.real_space_refine rotamer restrains? I mean rotamers { fit = all *outliers_or_poormap outliers_and_poormap outliers poormap restraints { enabled = True sigma = Auto target = max_distant min_distant exact_match fix_outliers } tuneup = outliers outliers_and_poormap } What is poormap? What is the range of Sigma? What are those types of target? With the latest nightly build, with default parameters starting model with 1% of rotamer outliers ends up with 10% (not using local_search, as it was done before). To minimise number of outliers, which parameters can be changed? Lower Sigma? Switch on tuneup? Thanks for any info! Leonid -- Prof. Leonid Sazanov FRS IST Austria Am Campus 1 A-3400 Klosterneuburg Austria Phone: +43 2243 9000 3026 E-mail: sazanov(a)ist.ac.at

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phenix.ligandfit, specifiy already generated cif file
by Guenter Fritz 22 Jan '21

22 Jan '21

Dear all, I would like to run phenix.ligandfit with a cif file I have already generated with acedrg or grade. This is not really required, just for comparison reasons. Would be nice. There is the parameter cif_already_generated= False / True But how do I define the cif file? Many thanks and best regards! Guenter

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Call for Abstracts: Michael G. Rossmann Memorial Symposium at the Microscopy & Microanalysis 2021
by Hasan, Syed Saif 20 Jan '21

20 Jan '21

Dear Colleagues, We cordially invite you to the “Michael G. Rossmann Memorial Symposium” at the Microscopy & Microanalysis 2021 conference, to be held in Pittsburgh, PA, Aug 1-5, 2021. This symposium focuses on the application of hybrid methods in electron microscopy of viruses, enzymes and other macromolecules, areas in which Michael was a pioneer. The symposium will feature invited talks from Prof. Hao Wu (Harvard Medical School), Prof. Rui Zhao (University of Colorado School of Medicine), and Prof. Chuan (River) Xiao (University of Texas El Paso). We invite abstracts from speakers in academics and industry at all career levels who develop and apply cutting-edge structural biology approaches to the study of viruses, viral proteins, enzymes, membrane proteins, and other systems. Ten abstracts will be selected for 15-minute oral presentations whereas the remaining abstracts will have the opportunity to be selected for poster presentations. Please note that the deadline for abstract submission is February 18, 2021. You will have the opportunity to select your preference for either in-person or virtual presentation. For additional meeting information and to register and submit your abstract, visit: https://www.microscopy.org/MandM/2021/ Deadline for abstract submission: February 18, 2021 We look forward to hosting you and learning about your exciting science at the M&M 2021 meeting. Sincerely, Terje Dokland (University of Alabama at Birmingham, Birmingham AL) S. Saif Hasan (University of Maryland School of Medicine, Baltimore MD)

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Retaining hydrogen in ligand while carrying out automatic ligand fitting.
by Rangarajan Erumbi 19 Jan '21

19 Jan '21

Hi, I am using phenix.ligandfit to automatically fit a ligand in to the ligand site of a protein model using the experimentally derived structure factors for the complex. The ligand pdb and restraints are created using phenix.elbow which contains the hydrogen atoms. However, after phenix.ligandfit the coordinates that are derived is stripped of all the ligand hydrogens. I want to retain the hydrogens only on the ligand during the refinement to preserve the overall geometry of the ligand. I am trying to do this automatically over several datasets with different ligands. I don’t see any specific parameter in the phenix.ligandfit that would specifically allow me to retain the ligand hydrogens. Phenix.reduce or phenix.ready_set does add hydrogens to entire coordinates including protein residues and so could not use it directly. Is there a way to get this accomplished in a simple way? Thanks in advance and appreciate your suggestions. Rangarajan.

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