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symmetry related bond restraint in R3 space group
by Xiang Li 11 Jan '13

11 Jan '13

I am trying to add some restraints between symmetric molecule with symmetry operation. However, I found it is not correct to use the operation information directly provided in Coot. The crystal I worked on has R3 symmetry. The symmetry operation in Coot shows to be -x+y,-x,z+ (1,1,0) and it did not work in Phenix refine. I read one previous email on this topic about the difference of symmetry operation in Coot and Phenix. However, I do not know how to do the conversion between the two when the numbers changed. Could you help me to work out on correct the symmetry operation in Phenix and talk some more on how to do the conversion please? I really appreciate your help! Sincerely, Xiang

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AutoSol error
by Luca Pellegrini 10 Jan '13

10 Jan '13

AutoSol (phenix 1.8.1-1168) stops at the build stage with the following message: *** ERROR MESSAGE: The cell appears to have changed during the run Original cell: [49.22, 91.325, 103.285, 113.16, 97.64000000000001, 76.74] New cell : [49.173301696777344, 92.32479858398438, 103.37100219726562, 66.54070281982422, 82.29070281982422, 76.58550262451172] If running from a script, please specify the space group in the input file. The incorrect space group may be coming from another wizard... *** Can you please advice as to what might be wrong? I am running AutoSol from the GUI and it did pick up the space group from the mtz file. What AutoSol refers to as the 'new cell' is actually my original cell. I was running two AutoSol jobs simultaneously from two mtz files with the same cell dimensions, and they both failed with the same message. Thanks, Luca Luca Pellegrini Department of Biochemistry University of Cambridge 80 Tennis Court Road Cambridge CB2 1GA - UK Email: lp212(a)cam.ac.uk Tel: 0044-1223-760469 Fax: 0044-1223-766002 Sanger building, room 3.59

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DEN refinement and reference model
by Luca Pellegrini 08 Jan '13

08 Jan '13

Phenix.den_refine (1.8.1-1168) stops and complains that: "Sorry: Reference model contains SEGIDs that do not match the working model." I have four chains in both working and reference model, ordered in the same way (A to D). Chains A and C are the same molecule, and chains B and D are also the same. Can you please advice? Some of the chains in the reference model contain more residues, is this a problem? Thanks for your help. Luca Luca Pellegrini Department of Biochemistry University of Cambridge 80 Tennis Court Road Cambridge CB2 1GA - UK Email: lp212(a)cam.ac.uk Tel: 0044-1223-760469 Fax: 0044-1223-766002 Sanger building, room 3.59

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dev-1261 wizard.test fail
by Morten Groftehauge 08 Jan '13

08 Jan '13

Hi guys, I just updated Rosetta to 3.4 and it seems to have compiled correctly (at least no error interruptions). I've done this enough to not be satisfied by that and ran > phenix_regression.wizards.test_command_line_rosetta_quick which goes past the Rosetta tests correctly but fails at ================================================================= Running test_prerefine ------------------------------------------------------------ Numbers do not match: 0.47825 0.53601 r {{ 0.87799 0.06946 -0.47362} {-0.02049 0.99396 0.10779} { 0.47825 -0.08494 0.87411}} --- r {{ 0.84375 0.06393 -0.53291} {-0.02789 0.99676 0.07541} { 0.53601 -0.04877 0.84280}} ------------------------------------------------------------ FAILED See log files test_prerefine/test_prerefine.log test_prerefine/test_prerefine_current.log ================================================================= Running test_prerefine_double OK ================================================================= Running test_prerefine_no_data ------------------------------------------------------------ Numbers do not match: 0.47825 0.53601 r {{ 0.87799 0.06946 -0.47362} {-0.02049 0.99396 0.10779} { 0.47825 -0.08494 0.87411}} --- r {{ 0.84375 0.06393 -0.53291} {-0.02789 0.99676 0.07541} { 0.53601 -0.04877 0.84280}} ------------------------------------------------------------ FAILED See log files test_prerefine_no_data/test_prerefine_no_data.log test_prerefine_no_data/test_prerefine_no_data_current.log ================================================================= When I look in the log there are no error messages. I don't need to prerefine so I'm good but I still find it weird. I tried again with Rosetta 3.3 and got no error flags. Is it because the quick tests are checking the result against the results that you got earlier and the algorithm has been changed between 3.3 and 3.4? Cheers, Morten PS Really enjoyed the talks at the CCP4 study weekend. -- Morten K Grøftehauge, PhD Pohl Group Durham University

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mr_rosetta and disulphide bonds
by Morten Groftehauge 07 Jan '13

07 Jan '13

Hello again, I forgot my important question in all my "this seems to be working but the test says it doesn't"-drama: How do I specify disulphide bonds for MR_rosetta? I know it keeps them if they are in the input model but disulphides are generally poorly conserved, especially in the %identity range where mr_rosetta is the most useful. According to the changelog this feature should be available in the latest dev. Cheers, Morten -- Morten K Grøftehauge, PhD Pohl Group Durham University

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Ph.D. position at Lund University
by Derek Logan 07 Jan '13

07 Jan '13

A 4-year PhD position is available in the groups of Dr. Derek Logan and Prof. Ulf Ryde at the Dept. of Biochemistry and Structural Biology and the Dept. of Theoretical Chemistry at Lund University, Sweden. The project is sponsored by the European Spallation Source and will also involve the participation of ESS scientists. The PhD student will work on structural and theoretical studies of protein-ligand interactions, using the carbohydrate binding protein galectin-3 as a model system. Structural studies will be conducted principally using neutron crystallography in combination with X-ray crystallography at very high resolution (< 0.9 Å). The work will include production of crystals of suitable size for neutron diffraction, data collection at various neutron sources around the world, data processing and modelling. The theoretical studies will be conducted in Ulf Ryde's group at Theoretical Chemistry. We will develop methods to combine crystallographic refinement and quantum mechanical calculations. In addition, we perform molecular dynamic simulations and estimates of binding affinities using free-energy perturbation. The project is part of a larger network at Lund University including organic chemists, medical scientists and NMR experts, dedicated to a fundamental understanding of protein-ligand interactions in general and galectin inhibition in particular. The candidate must have bachelor's degree in an appropriate subject (preferably chemistry) and should ideally have previous experience in structural biology, both theoretical and practical. The candidate should also have good knowledge of theoretical chemistry. Experience of quantum chemistry, statistical mechanics and simulations is an advantage. The deadline for application is 31st January 2013. For more information on the eligibility requirements, please see: http://admin.lu.se/o.o.i.s?id=22598&Dnr=511988&Type=E Application should be made using the link in the right hand column of this web page. For informal enquiries on the project contact: Derek Logan, Associate professor +46 46-2221443 derek.logan(a)biochemistry.lu.se Ulf Ryde, Professor +46-2224502 ulf.ryde(a)teokem.lu.se http://www.cmps.lu.se/ http://www.teokem.lu.se/ http://www.chem.lu.se/People/galectins_in_Lund/ http://www.esss.se

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Deadline: 4 February -- Please apply for RapiData 2013, a course on Data Collection and Structure Solving at the NSLS.
by Robert Sweet 04 Jan '13

04 Jan '13

We are offering RapiData 2013, the fifteenth offering of our popular course: Rapid Data Collection and Structure Solving at the NSLS: A Practical Course in Macromolecular X-Ray Diffraction Measurement The course will be held 21-26 April 2013: http://www.bnl.gov/RapiData/. Students could be at any level from advanced undergraduate to full professor. The course should accommodate 48 students total. We encourage all students to bring their own specimens for data collection, and to bring old data for the data-reduction and structure-solving tutorials. Please read the Course Announcement at http://www.bnl.gov/RapiData/. You'll see that many experts in the field will be available for lectures and tutorials. You'll find the application materials on the Course Application tab at this site. For the eleventh time we will hold a short lecture course on the fundamentals of crystallography for roughly five hours on Sunday 21 April. The body of the RapiData course really requires that students have a healthy knowledge of crystallography. For potential students who have some experience but are shaky about fundamentals, this course will help. There will be a small additional fee for the fundamentals course, to pay for Saturday night accomodations and food on Sunday morning and noon. Latin American Scientists: Several scholarships are available, from the International Union of Crystallography, to pay partial travel and subsistence costs for Latin-American students and junior faculty (under 40 yrs). Please apply for the course, and then contact R. Sweet (sweet(a)bnl.gov) if you are interested in applying for a scholarship. In accordance with the standards of the International Union of Crystallography, we observe the basic policy of non-discrimination, affirming the right and freedom of scientists to associate in international scientific activity without regard to such factors as citizenship, religion, creed, political stance, ethnic origin, race, colour, language, age, or gender, in accordance with the Statutes of the International Council for Science. At this course no barriers will exist beyond the application procedure that would prevent the participation of bona fide scientists. Please apply or send your students to our course, Bob Sweet, Sonya Kiss, and Alex Soares Course Announcement at http://www.bnl.gov/RapiData/ ========================================================================= Robert M. Sweet E-Dress: sweet(a)bnl.gov Group Leader, PXRR: Macromolecular ^ (that's L Crystallography Research Resource at NSLS not 1) http://px.nsls.bnl.gov/ Photon Sciences and Biology Dept Mail Stop, Bldg 463 Brookhaven Nat'l Lab. Phones: Upton, NY 11973 631 344 3401 (Office) U.S.A. 631 344 2741 (Facsimile) =========================================================================

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Fwd: WCPCW 21
by Nathaniel Echols 03 Jan '13

03 Jan '13

---------- Forwarded message ---------- From: "Williams, John Charles" <jwilliams(a)coh.org> To: "phenixbb(a)phenix-online.org" <phenixbb(a)phenix-online.org> Date: Thu, 3 Jan 2013 10:42:14 -0800 Subject: WCPCW 21 Dear All, Happy New Year! The West Coast Protein Crystallography Workshop is fast approaching (March 17th). The site (wcpcw.org) is up, registration is open and the option to pay by credit card is now available. The conference has a long tradition of methods development and organized as such to facilitate discussion and colloboration. We are especially interested in having speakers that are doing the ‘real’ work - graduate students, postdocs and staff scientists! We are also honored having Prof. Wayne Hendrickson as our keynote speaker. Prof. Hendrickson has made seminal contributions to the field including efforts in phase combination (Hendrickson-Lattman coefficients), incorporation of stereochemical constraints in protein refinement (e.g., PROLSQ – the predecessor to many of the refinement programs we now use), and the development of MAD phasing (including the development of selenomethionine incorporation). In addition, Prof. Hendrickson’s lab has produced a large number of biologically important structures including the HIV caspid GP120 bound to CD4, the first tyrosine kinase structure (Lck), and many, many others. We look forward to seeing you in Monterey! Best, John

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Anomalous group refinement question
by Pawel Grochulski 03 Jan '13

03 Jan '13

Dear all, Instruction says: Anomalous groups refines the anomalous coefficients f' and f'' for anomalously scattering atoms such as Se or heavy metals; it is only appropriate if you have anomalous data (I+/I- or F+/F-). How do I indicate which atoms to be considered? Thank you for your help. Happy New Year. Pawel ____________________ Dr. Pawel Grochulski, D.Sc. Canadian Macromolecular Crystallography Facility (cmcf.lightsource.ca<http://cmcf.lightsource.ca/>), Canadian Light Source Inc., 44 Innovation Boulevard, Saskatoon, SK S7N 2V3, Canada. Phone: +1 (306) 657-3538, Fax: +1 (306) 657-3535. Adjunct Professor of Pharmacy, College of Pharmacy and Nutrition, University of Saskatchewan (www.grochulski.com<http://www.grochulski.com/>) __________________________________________________________________________________________

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Problem with anomalous scattering factor refinement
by Subhani Bandara 26 Dec '12

26 Dec '12

Hi all, I've been trying to refine a structure with anomalous data with anomalous scattering factors. After some refinements without anomalous scattering factor refinement, I used the data.mtz file and original reflection file in reflection file editor to get the anomalous data merged with Rfree flags. When I tried to use this file with a pdb file (deleted hexadigest remark) and a cif file for ligands, the refinement ends with the following error at the end of the 3rd refinement cycle (I have only 3 cycles for a refinement). I was able to run a similar refinement with anomalous scattering factors for another structure without a problem. One difference in this structure is that this has NCS and the previous one didn't. I am using dev-1243 GUI. RuntimeError : scitbx array_family range error Traceback: File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/cctbx_project/libtbx/thread_utils.py", line 234, in run return_value = self._target(self._args, self._kwargs, self._c) File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/cctbx_project/libtbx/runtime_utils.py", line 87, in __call__ result = self.target() File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/cctbx_project/libtbx/runtime_utils.py", line 66, in __call__ result = self.run() File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/phenix/phenix/refinement/runtime.py", line 69, in run refine_object = self._run(args, callback) File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/phenix/phenix/refinement/runtime.py", line 85, in _run call_back_handler=callback) File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/phenix/phenix/refinement/command_line.py", line 169, in run map_manger.write_files() File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/phenix/phenix/refinement/driver.py", line 1735, in write_files map_coeff_dataset=self.write_mtz_file(), File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/phenix/phenix/refinement/driver.py", line 1724, in write_mtz_file pdb_hierarchy=self.refine_object.model.pdb_hierarchy()) File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/cctbx_project/mmtbx/maps/__init__.py", line 500, in __init__ pdb_hierarchy = pdb_hierarchy) File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/cctbx_project/mmtbx/maps/__init__.py", line 428, in map_coefficients_from_fmodel sharp = params.sharpening).map_coeffs File "/Applications/PHENIX-dev-1243/Contents/phenix-dev-1243/cctbx_project/mmtbx/map_tools.py", line 55, in __init__ data = self.map_coeffs.data()*scale) Thanks in advance for any help Subhani

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