December 2019 - 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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Adding a command line run job to the GUI job history
by Ahmad Khalifa 28 Dec '19

28 Dec '19

Hello, I ran a real space refinement job using the command line and an effective parameters file. Is it possible to link this job again to the Phenix GUI? How? Regards.

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Phenix Postdoc Position - Berkeley, California
by Paul Adams 24 Dec '19

24 Dec '19

Postdoctoral Researcher Lawrence Berkeley Laboratory Job ID: 89267 Division: Molecular Biophysics & Integrated Bioimaging (Computational Crystallography Initiative) Date Opened: 12/23/2019 Summary: Berkeley Lab’s Molecular Biophysics and Integrated Bioimaging Division has an opening for a Postdoctoral Researcher. In this role you will develop new computational methods for the structure determination and refinement of protein structures using the PHENIX software system. Primary duties and responsibilities will include development and implementation of numerical methods and new computational protocols, including the application of machine learning methods. The Phenix software is used worldwide for the determination of atomic structures using X-ray and neutron crystallography and cryo-electron microscopy. The software is developed as part of an international collaboration supported by the National Institutes of Health and the Phenix Industrial Consortium. To apply visit - https://lbl.taleo.net/careersection/2/jobdetail.ftl?job=89267 Duties: • Development and implementation of computational algorithms for structure determination using crystallography and cryo-electron microscopy including: improved methods for the optimization of models and automated detection of model heterogeneity. • Application of machine learning methods to problems in crystallography and cryo-electron microscopy. • Develop and test new components of the PHENIX software system in collaboration with others • Document software developments. • Collaborate with other researchers in the PHENIX program. • Interact with P.I.s, other postdocs, scientists and external collaborators involved in the PHENIX project. • Publication of research results in scientific journals and presentation of results at scientific meetings. Additional Responsibilities as needed: • Participate in workshop and tutorials to educate researchers in the use of Phenix • Actively participate in writing progress reports What is Required: • Ph.D. in computational crystallography, computational cryo-electron microscopy, computational biology, bioinformatics, computational chemistry or a related field • Demonstrated experience in developing computational algorithms for solving problems • Demonstrated experience with computational methods development • Publications in macromolecular crystallography, cryo-electron microscopy or closely related fields • Familiarity with Python, C++ and other software development tools • Good programming and mathematical skills • Strong interpersonal skills and the ability to work in a team environment Additional Desired Qualifications: • Familiarity with macromolecular structure or computational chemistry. • Experience with the practical aspects of crystallography and/or cryo-electron microscopy. The posting shall remain open until the position is filled. Notes: • This is a full time, 2 year postdoctoral appointment with the possibility of renewal based upon satisfactory job performance, continuing availability of funds and ongoing operational needs. You must have less than 3 years paid postdoctoral experience. Salary for Postdoctoral positions depends on years of experience post-degree. • Full-time, M-F, exempt (monthly paid) from overtime pay. • This position is represented by a union for collective bargaining purposes. • Salary will be predetermined based on postdoctoral step rates. • This position may be subject to a background check. Any convictions will be evaluated to determine if they directly relate to the responsibilities and requirements of the position. Having a conviction history will not automatically disqualify an applicant from being considered for employment. • Work will be primarily performed at: Lawrence Berkeley National Lab, 1 Cyclotron Road, Berkeley, CA. Learn About Berkeley Lab: Berkeley Lab (LBNL) addresses the world’s most urgent scientific challenges by advancing sustainable energy, protecting human health, creating new materials, and revealing the origin and fate of the universe. Founded in 1931, Berkeley Lab’s scientific expertise has been recognized with 13 Nobel prizes. The University of California manages Berkeley Lab for the U.S. Department of Energy’s Office of Science. Working at Berkeley Lab has many rewards including a competitive compensation program, excellent health and welfare programs, a retirement program that is second to none, and outstanding development opportunities. To view information about the many rewards that are offered at Berkeley Lab- Click Here. Equal Employment Opportunity: Berkeley Lab is an Equal Opportunity/Affirmative Action Employer. All qualified applicants will receive consideration for employment without regard to race, color, religion, sex, sexual orientation, gender identity, national origin, disability, age, or protected veteran status. Berkeley Lab is in compliance with the Pay Transparency Nondiscrimination Provision under 41 CFR 60-1.4. Click here to view the poster and supplement: "Equal Employment Opportunity is the Law. -- 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 347 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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NIH-Funded Post-Doctoral Position at the University of Illinois to Study the Ribosome Structure
by Yury Polikanov 18 Dec '19

18 Dec '19

*NIH-Funded Post-Doctoral Position in Structural Biology at the University of Illinois at Chicago (UIC) to Study the Structure and Function of the Ribosome* [image: Movie_S3_70S-mtRNA_320x240.gif] The Polikanov Laboratory at the University of Illinois at Chicago (IL, USA) is looking for a talented, skillful, and highly motivated researcher to fill the available *NIH-funded Post-Doctoral Scholar *position 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 and potentially cryo-EM 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:* - 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. *In the cover letter, the applicant should **describe how his/her previous research accomplishments and scientific interests fit with the scope of the research in the Polikanov research group.* -- ------------------------------ 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: Image result for uic logo] ------------------------------

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PhD / PostDoc positions @NKI Amsterdam
by a.perrakis＠nki.nl 18 Dec '19

18 Dec '19

Dear all, We are looking for enthusiastic, motivated PhD students and Post-Docsto join the Division of Biochemistry in the Netherlands Cancer Institute (https://www.nki.nl) in the groups of Tassos Perrakis and Titia Sixma. If you have a keen interest in the general field of integrative structural cell biology, and previous experience in cryo-EM, X-ray crystallography, cell biology, biochemistry, or biophysics … well, read on! The project in the laboratory of Titia Sixma (https://www.nki.nl/divisions/biochemistry/sixma-t-group/ ) is in the area of DNA repair. The projects in Anastassis (Tassos) Perrakis group (https://www.nki.nl/divisions/biochemistry/perrakis-a-group/) are in the general field of controlling the progress of cell division and microtubule interacting proteins, in lysolipids signaling focusing on Autotaxin and its interactions, and together with Robbie Joosten in PDB-REDO . The Netherlands Cancer Institute is an international center of excellence with a high standard of biological research and outstanding research facilities, and has an interactive atmosphere. It is located in Amsterdam, with all its cultural amenities, close to the Schiphol airport. The two groups share a common research infrastructure in the Department of Biochemistry, and have an interest in structural studies coupled to functional analysis. Facilities include the ability to produce and purify proteins in bacterial, insect, and mammalian cells, and a well-equipped macromolecular biophysics laboratory that are sites in the Instruct Centre NL (https://instruct-eric.eu/centre/protein-facility---nki/). Equipment for structural analysis is spearheaded by a brand-new cryo-EM (Jeol F2 200kV with a K2 detector) and high-throughput crystallisation robotics; these local facilities are coupled with regular access to Krios cryo-EM at NeCEN (https://www.necen.nl , https://instruct-eric.eu/centre/necen---lu/) and to the ESRF, SLS and DLS synchrotrons, and access possibilities for NMR experiments (https://instruct-eric.eu/centre/bijvoet-center---uu/). Dedicated computing facilities include privileged access to both CPU and GPU clusters. Both groups participate in various European and National collaborative projects and are members of the Oncode Institute (https://www.oncode.nl). We are looking flexibly for either highly motivated PhD students (strong master-level placements in reputable laboratories and familiarity with some of the methods we outline would be strong plus) or post-docs (experience in cryo-EM would be highly desirable for most positions; candidates with a strong background and track record in X-ray crystallography, protein purification, cell biology, would be taken seriously under considerations depending on the project). For the PDB-REDO project a background in bioinformatics and some experience in computerprogramming would be necessary. Applicants should write an email, stating their specific interests and attaching a CV and names of three references to t.sixma.AT.nki.nl or a.perrakis.AT.nki.nl; feel free to also make informal inquiries. We expect applications to be sent in by Monday 13th January and all positions are available asap. PhD candidate positions are for four years; post-doc positions can be for 1-4 years depending on qualifications and experience; the CAO salary levels apply according to the NKI collective agreement. Anastassis Perrakis and Titia K. Sixma

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First CCP4 Study Weekend illustration competition
by Jon Agirre 16 Dec '19

16 Dec '19

Dear colleagues, We are pleased to announce the opening of the first CCP4 Study Weekend illustration competition, made possible by CCP4’s long standing collaboration with IUCr Journals. Getting your science out to the public requires more than good research. You need to make it memorable! And what better way to do it than with excellent figures? We invite you to make a figure that tells a structural biology story in a creative and informative way. The submitted figures will be showcased during the Study Weekend at several locations at the conference venue. *Prize* The creator of the winning illustration gets to design the cover illustration of the Study Weekend’s proceedings to be published early 2021. Apart from this commission there may be another (sur)prize. *Format* Illustrations, along with a short description of content and methods used, are to be sent to jon.agirre(a)york.ac.uk before December 15th 2019. Images must have a resolution of 1920x1080 (16:9) in order to fit the format of the screens and main room projector. Any combination of graphics and (if any) post-processing software may be used, as long as details are given with the submission. The format of the illustration should be PNG. *Judges* As you may know, Dr Jeroen Claus (founder of Phospho Biomedical Animation) will give the closing talk at the 2020 edition of the CCP4 Study Weekend. He, along with Louise Jones (managing editor of Acta Crystallographica sections D & F) will judge the submitted figures based on their graphical quality as well as their ability to convey a complex structural message clearly. *Decision* The winner will be announced on January 8th at the dinner - before the céilidh. Up to date information and registration: http://www.cvent.com/d/fyq0g9/4K?cpc=FCNF5V7H4B4 Looking forward to receiving your images! Jon Agirre, Alan Roseman, Robbie Joosten and Karen McIntyre -- Dr Jon Agirre Royal Society University Research Fellow York Structural Biology Laboratory / Department of Chemistry University of York, Heslington, YO10 5DD, York, UK http://www.york.ac.uk/chemistry/research/ysbl/people/staff/jagirre/ Office: /B/K/065 Phone: +44 (0) 1904 32 8252 Twitter: @glycojones

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Emergency power test at Berkeley this weekend (12/13-12/16)
by Billy Poon 14 Dec '19

14 Dec '19

Hi everyone, To mitigate disruptions from future power shut offs due to wildfire concerns, we are performing an emergency power test for our web servers. This will affect the phenix-online.org and cci.lbl.gov servers. The websites, mailing lists, and repositories will remain available, but the servers will be running on emergency power instead. The servers will be switched to emergency power at around 2 pm Pacific time on Friday (12/13) and switched back to main power around 10 am Pacific time on Monday (12/16). Please let me know if you experience any issues. Thanks! -- Billy K. Poon Research Scientist, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory 1 Cyclotron Road, M/S 33R0345 Berkeley, CA 94720 Tel: (510) 486-5709 Fax: (510) 486-5909 Web: https://phenix-online.org

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Re: [phenixbb] map to model fsc did not start from 1
by BuddySphinx 12 Dec '19

12 Dec '19

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map to model fsc did not start from 1
by Yangqi Gu 12 Dec '19

12 Dec '19

Dear Phenix developer, I have a question regarding the map to model fsc. I have a filament map and a model with arbitrary copy of the protomer ( I built them in Chimera), then I used the filament model to refine against my map. But I encountered an issue is that the reported FSC (map to model) did not start from 1 but rather 0.8. I am wondering if there is anyway to fix it. Also, in the case of a filament, how do I use NCS operator to refine rather than manual building the filament model? I tried specifying NCS with helical symmetry, but it did not work. Best, Yangqi

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Re: [phenixbb] problems running refinement of shaken model against half map
by L. Hielkema 07 Dec '19

07 Dec '19

Dear Pavel, Thanks again for your answer. I understand that you have some concerns with regard to the validation we use. Now this makes me really curious how the rest of the EM community feels about this. > "widely used" does not always mean "makes sense". As it often happens, some may just blindly follow the crowd. And how "widely" it is used, in fact? I stated my arguments as to why this does not make sense (to me at least). I'm yet to hear any strong counter-arguments. > So you stated the following before: "First off, I think this way of validation is quite faulty conceptually... How you know 0.5A is the best number and say not 0.7 or 0.3? By shaking the model, you validate the shaken (perturbed) model, which is not the model you are publishing and reporting statistics for. If you shake the model twice with same shake doze, you will get two different models with the same amount of perturbation, which means numbers you derive from such models can (and likely will) be different.” Is there anyone that would have any strong counter arguments? Or thinks along the same way? Because we would really like to know if we should change anything in our approach. Or would then the approach that Pavel suggest with the phenix tool Comprehensive validation be a good solution to this issue? > The paper you refer to indeed describes the protocol they followed but it does not answer concerns that I raised before. > > History knows plenty of examples of something being almost a standard for a while and then discarded later. Such as cutting off low-resolution diffraction data (because at the time there was no good bulk-solvent models invented) or cutting data by 2 or 3 "sigma" criteria (because maximum-likelihood target functions were not in use yet), etc etc etc. Or not adding H atoms to atomic models... > > Cryo-EM isn't as mature as protein crystallography where most procedures and protocols are pretty much standard. Cross validation for cryo-EM is yet to settle to some more meaningful method. There is indeed a number of attempts made so far but none of them seem to be as good as Brunger's free-R approach! Sure many things have to be still established, but it would be nice to know what is the generally accepted method at the moment according to the community. > >> As far as I could see the phenix tool Comprehensive validation did not provide the validation against the half maps, that one needs to obtain FSCwork and FSCfree, which is described in the attached papers. > > This is correct, it doesn't for reasons I mentioned before. Best, Lisa > On 5 Dec 2019, at 21:02, Pavel Afonine <pafonine(a)lbl.gov> wrote: > > Hi Lisa, > >> Thanks for your answer. Though I am a bit confused, as far as I and my group understand this method is widely used for several years (see attached papers for first introduction and since then you see many performing this type of validation). > > "widely used" does not always mean "makes sense". As it often happens, some may just blindly follow the crowd. And how "widely" it is used, in fact? I stated my arguments as to why this does not make sense (to me at least). I'm yet to hear any strong counter-arguments. > > The paper you refer to indeed describes the protocol they followed but it does not answer concerns that I raised before. > > History knows plenty of examples of something being almost a standard for a while and then discarded later. Such as cutting off low-resolution diffraction data (because at the time there was no good bulk-solvent models invented) or cutting data by 2 or 3 "sigma" criteria (because maximum-likelihood target functions were not in use yet), etc etc etc. Or not adding H atoms to atomic models... > > Cryo-EM isn't as mature as protein crystallography where most procedures and protocols are pretty much standard. Cross validation for cryo-EM is yet to settle to some more meaningful method. There is indeed a number of attempts made so far but none of them seem to be as good as Brunger's free-R approach! > >> As far as I could see the phenix tool Comprehensive validation did not provide the validation against the half maps, that one needs to obtain FSCwork and FSCfree, which is described in the attached papers. > > This is correct, it doesn't for reasons I mentioned before. > > All the best, > Pavel >

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