- phenixbb - phenix-online.org

Table 1 successor in 3D?
by Gerard Bricogne 13 Jun '18

13 Jun '18

Dear phenixbb subscribers, I sent the message below to the CCP4BB and phenixbb at the same time last Friday. It went straight through to the CCP4BB subscribers but was caught by the phenixbb Mailman because its size exceeded 40K. Nigel, as moderator of this list, did his best to rescue it, but all his attempts failed. He therefore asked me to resubmit it, now that he has increased the upper size limit. Apologies to those of you who are also CCP4BB subscribers, who will already have received this message and the follow-up discussion it has given rise to. With best wishes, Gerard. ----- Forwarded message from Gerard Bricogne <gb10> ----- Date: Fri, 1 Jun 2018 17:30:48 +0100 From: Gerard Bricogne <gb10> Subject: Table 1 successor in 3D? To: CCP4BB(a)JISCMAIL.AC.UK, phenixbb(a)phenix-online.org Dear all, Bernhard Rupp has just published a "Perspective" article in Structure, accessible in electronic form at https://www.cell.com/structure/fulltext/S0969-2126(18)30138-2 in which part of his general argument revolves around an example (given as Figure 1) that he produced by means of the STARANISO server at http://staraniso.globalphasing.org/ . The complete results of his submission to the server have been saved and may be accessed at http://staraniso.globalphasing.org/Gallery/Perspective01.html and it is to these results that I would like to add some annotations and comments. To help with this, I invite the reader to connect to this URL, type "+" a couple of times to make the dots bigger, and press/toggle "h" whenever detailed information on the display, or selection of some elements, or the thresholds used for colour coding the displays, needs to be consulted. The main comment is that the WebGL interactive 3D display does give information that makes visible characteristics that could hardly be inferred from the very condensed information given in Table 1, and the annotations will be in the form of a walk through the main elements of this display. For instance the left-most graphical object (a static view of which is attached as "Redundancy.png") shows the 3D distribution of the redundancy (or multiplicity) of measurements. The view chosen for the attached picture shows a strong non-uniformity in this redundancy, with the region dominated by cyan/magenta/white having about twice the redundancy (in the 6/7/8 range) of that which prevails in the region dominated by green/yellow (in the 3/5 range). Clear concentric gashes in both regions, with decreased redundancy, show the effects of the inter-module gaps on the Pilatus 2M detector of the MASSIF-1 beamline. The blue spherical cap along the a* axis corresponds to HKLs for which no measurement is available: it is clearly created by the detector being too far from the crystal. The second (central) graphical object, of which a view is given in Figure 1 of Bernhard's article and another in the attached picture "Local_I_over_sigI.png") shows vividly the blue cap of measurements that were missed but would probably have been significant (had they been measured) cutting into the green region, where the local average of I/sig(I) ranges between 16 and 29! If the detector had been placed closer, significant data extending to perhaps 3.0A resolution would arguably have been measured from this sample. The right-most graphical object (of which a static view is attached as "Debye-Waller.png") depicts the distribution of the anisotropic Debye-Waller factor (an anisotropic generalisation of the Wilson B) of the dataset, giving yet another visual hint that good data were truncated by the edges of a detector placed too far. Apologies for such a long "STARANISO 101" tutorial but Bernhard's invitation to lift our eyes from the terse numbers in Table 1 towards 3D illustrations of data quality criteria was irresistible ;-) . His viewpoint also agrees with one of the main purposes of our STARANISO developments (beyond the analysis and remediation of anisotropy, about which one can - and probably will - argue endlessly) namely contribute to facilitating a more direct and vivid perception by users of the quality of their data (or lack of it) and to nurturing evidence-based motivation to make whatever extra effort it takes to improve that quality. In this case, the undeniable evidence of non-uniformity of redundancy and of a detector placed too far would give immediate practical guidance towards doing a better experiment, while statistics in Table 1 for the same dataset would probably not ... . Thank you Bernhard! With best wishes, Gerard, for and on behalf of the STARANISO developers ----- End forwarded message -----

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Coupling ligand occupancy with helix displacement
by John Michael Bruning 11 Jun '18

11 Jun '18

Hi, I have a very flexible covalent adduct that adopts three alternative conformations (A,B,C) in my structure . Conformations A and C are solvent exposed, while conformation B is buried. The buried conformation B displaces a regulatory helix (resseq 589:598) by a few angstrom, while the solvent exposed conformations do not displace this helix. I can't seem to write a occupancy .params file that fulfills: 1.) occ. of ligand conformation B = occ. of displaced helix conformation # coupling of ligand binding with helix displacement 2.) occ. non-displaced helix conformation = (1 - occ. displaced helix conformation) 3.) sum occ. ligand conformations A+B+C = 1 # assuming protein was initially labeled 100% It seems like #7 from http://www.phenix-online.org/newsletter/CCN_2015_07.pdf#page=12 is my situation, but I can't quite seem to modify this for my case. For example, something like: constrained_group { selection = chain A and resname CPE and altid B or chain A and resseq 589:598 and altid B} Captures the concerted conformation aspect (1) (occupancy for ligand conformation B = occupancy for displaced helix) and the sum occupancy of the displaced and non-displaced helix = 1 (2), but the sum of the the alternative conformations A+B+C > 1.0 (w/ A+C = 1.0) (3) Incidentally, my resolution is 2.4 Ang. Thanks for any help! Cheers, John Cheers, John *********************************** John Bruning, Post-Doctoral Scholar Stanford University, Glenn Lab CCSR Building, #3110 ***********************************

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CSHL X-ray Methods in Structural Biology Course Oct 15-30th 2018: Application deadline June 15th
by Paul Adams 05 Jun '18

05 Jun '18

Dear Colleagues, 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 2018, is rapidly approaching. This is a unique opportunity to become expert in the use of X-ray crystallography to solve challenging macromolecular structures. The official course announcement can be found here: https://meetings.cshl.edu/courses.aspx?course=C-CRYS&year=18 please pass this on to people who might be interested and who would benefit, including your students and postdocs. This comprehensive course is an outstanding place to learn both the theoretical and practical aspects of macromolecular crystallography, and consists of extensive lectures and practical sessions from experts in the field. The instructor team is: Alex McPherson, Bill Furey, Jim Pflugrath, Tassos Perrakis, and myself. We are assisted by world recognized experts in crystallization, data collection, data processing, structure solution, refinement, and validation (see the course link above for more details). The goal of the course is for researchers who have had some exposure to X-ray crystallography to become experts. This is an experience in macromolecular crystallography learning that cannot be found anywhere else, and the student/teacher ratio is often 1:1. We expect participants to crystallize one or more proteins and determine their structures in a two week period. Students may also work on their own projects, but not exclusively. They will become very well-versed in the theory of X-ray diffraction and crystal structure determination, while also having lots of fun. Both synchrotron data collection and in-house diffraction data collection will be used to solve structures. The course is limited to 16 participants due to the very hands-on nature of the experiments and the intimate seminar and laboratory settings. Please check the above web link for more details. In particular, please note the information about the various fellowships, scholarships, and stipends that are available. The 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 an e-mail, we will be happy to answer all queries. 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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Fwd: phenixbb post from [email protected]
by Nigel Moriarty 04 Jun '18

04 Jun '18

Folks There was a post from Gerard Bricogne that was lost (as far as I can see) in the internals of MailMan because of a 40Kb size limit and other reasons unknown. It was posted to the CCP4BB so you may have already seen it. Please find it below. 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 Subject: Table 1 successor in 3D? Dear all, Bernhard Rupp has just published a "Perspective" article in Structure, accessible in electronic form at https://www.cell.com/structure/fulltext/S0969-2126(18)30138-2 in which part of his general argument revolves around an example (given as Figure 1) that he produced by means of the STARANISO server at http://staraniso.globalphasing.org/ . The complete results of his submission to the server have been saved and may be accessed at http://staraniso.globalphasing.org/Gallery/Perspective01.html and it is to these results that I would like to add some annotations and comments. To help with this, I invite the reader to connect to this URL, type "+" a couple of times to make the dots bigger, and press/toggle "h" whenever detailed information on the display, or selection of some elements, or the thresholds used for colour coding the displays, needs to be consulted. The main comment is that the WebGL interactive 3D display does give information that makes visible characteristics that could hardly be inferred from the very condensed information given in Table 1, and the annotations will be in the form of a walk through the main elements of this display. For instance the left-most graphical object (a static view of which is attached as "Redundancy.png") shows the 3D distribution of the redundancy (or multiplicity) of measurements. The view chosen for the attached picture shows a strong non-uniformity in this redundancy, with the region dominated by cyan/magenta/white having about twice the redundancy (in the 6/7/8 range) of that which prevails in the region dominated by green/yellow (in the 3/5 range). Clear concentric gashes in both regions, with decreased redundancy, show the effects of the inter-module gaps on the Pilatus 2M detector of the MASSIF-1 beamline. The blue spherical cap along the a* axis corresponds to HKLs for which no measurement is available: it is clearly created by the detector being too far from the crystal. The second (central) graphical object, of which a view is given in Figure 1 of Bernhard's article and another in the attached picture "Local_I_over_sigI.png") shows vividly the blue cap of measurements that were missed but would probably have been significant (had they been measured) cutting into the green region, where the local average of I/sig(I) ranges between 16 and 29! If the detector had been placed closer, significant data extending to perhaps 3.0A resolution would arguably have been measured from this sample. The right-most graphical object (of which a static view is attached as "Debye-Waller.png") depicts the distribution of the anisotropic Debye-Waller factor (an anisotropic generalisation of the Wilson B) of the dataset, giving yet another visual hint that good data were truncated by the edges of a detector placed too far. Apologies for such a long "STARANISO 101" tutorial but Bernhard's invitation to lift our eyes from the terse numbers in Table 1 towards 3D illustrations of data quality criteria was irresistible ;-) . His viewpoint also agrees with one of the main purposes of our STARANISO developments (beyond the analysis and remediation of anisotropy, about which one can - and probably will - argue endlessly) namely contribute to facilitating a more direct and vivid perception by users of the quality of their data (or lack of it) and to nurturing evidence-based motivation to make whatever extra effort it takes to improve that quality. In this case, the undeniable evidence of non-uniformity of redundancy and of a detector placed too far would give immediate practical guidance towards doing a better experiment, while statistics in Table 1 for the same dataset would probably not ... . Thank you Bernhard! With best wishes, Gerard, for and on behalf of the STARANISO developers

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d99 beyond Nyquist?
by Ricardo Righetto 03 Jun '18

03 Jun '18

Hi, I've seen the d99 criterion in phenix.mtriage reporting a resolution value beyond Nyquist (=2.0 A), or very close to Nyquist in another case. For these particular maps, which are from the same dataset processed with two different single-particle analysis packages (internal benchmarking), half-map FSC-based methods (including blocres) report resolutions in the range of 3.0-3.5 A which are consistent with the features I can see. How can I interpret this? I understand that d99 starts omitting Fourier samples from the corners of the reciprocal box, but does it make sense to report a value beyond Nyquist? I tried supplying unfiltered, masked and unmasked versions of the maps with barely any variation in the d99 results. Thanks in advance for helping figuring this out! Best wishes, -- Ricardo Diogo Righetto

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Computational Crystallography Newsletter (CCN) submissions
by Nigel Moriarty 01 Jun '18

01 Jun '18

Folks Calling for articles and short communications of interest to structural biologists. The initial deadline for submission for the July 2018 issue is 22 June 2018. 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. 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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Table 1 successor in 3D?
by Gerard Bricogne 01 Jun '18

01 Jun '18

Dear all, Bernhard Rupp has just published a "Perspective" article in Structure, accessible in electronic form at https://www.cell.com/structure/fulltext/S0969-2126(18)30138-2 in which part of his general argument revolves around an example (given as Figure 1) that he produced by means of the STARANISO server at http://staraniso.globalphasing.org/ . The complete results of his submission to the server have been saved and may be accessed at http://staraniso.globalphasing.org/Gallery/Perspective01.html and it is to these results that I would like to add some annotations and comments. To help with this, I invite the reader to connect to this URL, type "+" a couple of times to make the dots bigger, and press/toggle "h" whenever detailed information on the display, or selection of some elements, or the thresholds used for colour coding the displays, needs to be consulted. The main comment is that the WebGL interactive 3D display does give information that makes visible characteristics that could hardly be inferred from the very condensed information given in Table 1, and the annotations will be in the form of a walk through the main elements of this display. For instance the left-most graphical object (a static view of which is attached as "Redundancy.png") shows the 3D distribution of the redundancy (or multiplicity) of measurements. The view chosen for the attached picture shows a strong non-uniformity in this redundancy, with the region dominated by cyan/magenta/white having about twice the redundancy (in the 6/7/8 range) of that which prevails in the region dominated by green/yellow (in the 3/5 range). Clear concentric gashes in both regions, with decreased redundancy, show the effects of the inter-module gaps on the Pilatus 2M detector of the MASSIF-1 beamline. The blue spherical cap along the a* axis corresponds to HKLs for which no measurement is available: it is clearly created by the detector being too far from the crystal. The second (central) graphical object, of which a view is given in Figure 1 of Bernhard's article and another in the attached picture "Local_I_over_sigI.png") shows vividly the blue cap of measurements that were missed but would probably have been significant (had they been measured) cutting into the green region, where the local average of I/sig(I) ranges between 16 and 29! If the detector had been placed closer, significant data extending to perhaps 3.0A resolution would arguably have been measured from this sample. The right-most graphical object (of which a static view is attached as "Debye-Waller.png") depicts the distribution of the anisotropic Debye-Waller factor (an anisotropic generalisation of the Wilson B) of the dataset, giving yet another visual hint that good data were truncated by the edges of a detector placed too far. Apologies for such a long "STARANISO 101" tutorial but Bernhard's invitation to lift our eyes from the terse numbers in Table 1 towards 3D illustrations of data quality criteria was irresistible ;-) . His viewpoint also agrees with one of the main purposes of our STARANISO developments (beyond the analysis and remediation of anisotropy, about which one can - and probably will - argue endlessly) namely contribute to facilitating a more direct and vivid perception by users of the quality of their data (or lack of it) and to nurturing evidence-based motivation to make whatever extra effort it takes to improve that quality. In this case, the undeniable evidence of non-uniformity of redundancy and of a detector placed too far would give immediate practical guidance towards doing a better experiment, while statistics in Table 1 for the same dataset would probably not ... . Thank you Bernhard! With best wishes, Gerard, for and on behalf of the STARANISO developers

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Anisotropy with TLS
by Eugene Osipov 31 May '18

31 May '18

Hi, everyone, Can someone shed a light on B-factor refinement in PHENIX.refine. I am refining the structure with 2.5 A resolution, with individual B-factors and automatically defined TLS groups. Despite isotropic refinement of B-factors I still see ANISOU entries for atoms. I figured out that these ANISOU lines appear only after TLS refinement. So the question is how these ANISOU values are calculated? -- Eugene Osipov Junior Research Scientist Laboratory of Enzyme Engineering A.N. Bach Institute of Biochemistry Russian Academy of Sciences Leninsky pr. 33, 119071 Moscow, Russia e-mail: e.m.osipov(a)gmail.com

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Berkeley Server Downtown (5/29 - 5/31)
by Billy Poon 30 May '18

30 May '18

Dear all, On Tuesday, May 29, our servers will be shut down starting at 5:00 pm Pacific for scheduled maintenance in our building. We expect that the servers will be available by 10:00 am Pacific on Thursday (5/31) at the latest. This will affect, - The Phenix web site (http://phenix-online.org/) - The DIALS West web site (http://dials.lbl.gov/) - The CCI web site (http://cci.lbl.gov/) - The Structural Biology Technology Portal (http://technology.sbkb.org/) Bug reports and emails requesting help should be queued and we will receive them once the servers are back online. We apologize for any inconvenience. -- 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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postdoc crystallographer job offer; International Institute in Warsaw, 15th Jun
by Błażej Bagiński 30 May '18

30 May '18

Dear All, Bujnicki Lab (Laboratory if Bioinformatics and Protein Engineering, located in the International Institute of Molecular and Cell Biology in Warsaw) is looking for an experienced (post-doc level) crystallographer/structural biologist, with an interest in combining various experimental and computational methods for structure determination of RNAs and RNA-protein complexes. Our group is involved in theoretical and experimental research on nucleic acids and proteins. The current focus is on RNA sequence-structure-function relationships (in particular 3D modeling), RNA-protein complexes, and enzymes acting on RNA. The Institute have in-house crystallographic and computing facilities and is located in the Ochota campus, surrounded by Polish Academy of Science's institutes and University of Warsaw's departments of biology/chemistry/physics/medicine/mathematics interests. Please find the full job offer in the attachment, as well as in the link below. The deadline is on 15th of June 2018. http://genesilico.pl/employment/#5 The webpage of our group can be found here; http://genesilico.pl/ as well as more information about the Institute: https://www.iimcb.gov.pl/en/ For more information and questions, please contact this address: Bujnicki, Janusz: iamb(a)genesilico.pl Kind regards, Błażej Bagiński

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