- phenixbb - phenix-online.org

(no subject)
by Tom Burnley 18 Apr '12

18 Apr '12

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Re: [phenixbb] Bulk Solvent
by Nathaniel Echols 17 Apr '12

17 Apr '12

Garib's response below, since the server wouldn't let him post. ---------- Forwarded message ---------- From: Garib N Murshudov <garib(a)MRC-LMB.CAM.AC.UK> To: "Steiner, Roberto" <roberto.steiner(a)kcl.ac.uk> Cc: PHENIX user mailing list <phenixbb(a)phenix-online.org> Date: Tue, 17 Apr 2012 18:11:24 +0100 Subject: Re: [phenixbb] Bulk Solvent Dear all I cannot say much without data. Only thing I can say that there were some problems in some of the versions in 5.5, and there are some improvements in recent versions. 5.7 series may perform better. Before claiming that improvement is due to particular feature I would do a little bit more analysis. regards Garib On 17 Apr 2012, at 18:03, Steiner, Roberto wrote: difference density on the backbone can also arise (more often) due to suboptimal ADP refinement/restraints..or a bug in a particular build.. best wishes roberto PS I cc-ed this email to Garib in case he's got some info specific for 5.5.0102 On 17 Apr 2012, at 17:22, Timothy Springer wrote: As I said, I cant say that, it is a guess based on two facts. 1) Looking at the output of refinement steps, and seeing that the largest decrease in R during refinement comes in the bulk solvent correction step. 2) It is also based on the common occurrence in the Refmac but not Phenix maps of negative difference density on backbone. This is a symptom of errors in bulk solvent correction. Tim On Apr 17, 2012, at 12:06 PM, Steiner, Roberto wrote: Hi Tim, How can you say the difference is really down to bulk solvent correction? there's several other parameters that affect differences in R factors.... Just curious R On 17 Apr 2012, at 16:27, Timothy Springer wrote: no, it just takes me two years to write up sometimes--- So this is a historical question. But there is a ref in that powerpoint to following ref. If this was implemented in Phenix and not Refmac 2 years ago, I should cite it. Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):850-5. Epub 2005 Jun 24. A robust bulk-solvent correction and anisotropic scaling procedure. Afonine PV, Grosse-Kunstleve RW, Adams PD. Source Lawrence Berkeley National Laboratory, One Cyclotron Road, Building 64R0121, Berkeley, CA 94720, USA. pafonine(a)lbl.gov Tim On Apr 17, 2012, at 11:18 AM, Jeff Headd wrote: Hi Tim, If you are using Phenix 1.5.2, that would not have had the new bulk-solvent model that Pavel is talking about. Are you using that old of a version for your tests? Jeff On Tue, Apr 17, 2012 at 8:07 AM, Pavel Afonine <pafonine(a)lbl.gov> wrote: > > Hi Tim, > > this is because recently (a few weeks ago) we introduced a novel bulk-solvent model and a new overall anisotropic scaling procedure. > > Some detailed overview is here: > > http://www.phenix-online.org/presentations/PhenixSantaFe2012_PA.pdf > > This is going to be published soon. > > Pavel > > > On 4/17/12 7:59 AM, Timothy Springer wrote: > > In one of the structures I have refined, I found phenix 1.5_2 gave 1 to 1.5% lower Rfree and Rwork than REFMAC 5.5.0102. > Can I propose in a publication that "We attribute these differences to methods for handling bulk solvent in PHENIX that are less adversely affected by deficiencies in the crystallographic data."? > This is a guess, because there is a large contribution to refinement from bulk solvent, rather than factual information. I did cross-refinement, and found it going from structures refined in REfmac to Phenix, and vice versa. The Phenix maps looked better, too. > Is this a reasonable suggestion, and would there be a relevant reference? > Tim > > > > _______________________________________________ > phenixbb mailing list > phenixbb(a)phenix-online.org > http://phenix-online.org/mailman/listinfo/phenixbb > _______________________________________________ phenixbb mailing list phenixbb(a)phenix-online.org http://phenix-online.org/mailman/listinfo/phenixbb <ATT00001..c> Roberto Steiner, PhD Group Leader Randall Division of Cell and Molecular Biophysics King's College London Room 3.10A New Hunt's House Guy's Campus SE1 1UL, London, UK Tel 0044-20-78488216 Fax 0044-20-78486435 roberto.steiner(a)kcl.ac.uk _______________________________________________ phenixbb mailing list phenixbb(a)phenix-online.org http://phenix-online.org/mailman/listinfo/phenixbb <ATT00001..c> Roberto Steiner, PhD Group Leader Randall Division of Cell and Molecular Biophysics King's College London Room 3.10A New Hunt's House Guy's Campus SE1 1UL, London, UK Tel 0044-20-78488216 Fax 0044-20-78486435 roberto.steiner(a)kcl.ac.uk Dr Garib N Murshudov Group Leader, MRC Laboratory of Molecular Biology Hills Road Cambridge CB2 0QH UK Email: garib(a)mrc-lmb.cam.ac.uk Web http://www.mrc-lmb.cam.ac.uk

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Bulk Solvent
by Timothy Springer 17 Apr '12

17 Apr '12

In one of the structures I have refined, I found phenix 1.5_2 gave 1 to 1.5% lower Rfree and Rwork than REFMAC 5.5.0102. Can I propose in a publication that "We attribute these differences to methods for handling bulk solvent in PHENIX that are less adversely affected by deficiencies in the crystallographic data."? This is a guess, because there is a large contribution to refinement from bulk solvent, rather than factual information. I did cross-refinement, and found it going from structures refined in REfmac to Phenix, and vice versa. The Phenix maps looked better, too. Is this a reasonable suggestion, and would there be a relevant reference? Tim

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Re: [phenixbb] Sugar woes
by Matthew J. Whitley 17 Apr '12

17 Apr '12

Hi Simon, I have been struggling with very similar issues over the last few weeks, but I (finally!) got it to work appropriately using just the procedure you described. In my case, I was trying to fit and refine a pentasaccharide consisting of MAN and BMA. Adapting what I did to your case, I would suggest the following steps: After loading NAG and MAN monomers into Coot and manually placing them into the electron density in approximately correct positions, save the coordinates and then manually delete the appropriate hydrogens and oxygen from the PDB file. You specifically stated that you did NOT remove the hydrogens, but I found it to be absolutely necessary to delete these atoms, even though my feeling is that Phenix is supposed to remove automatically the appropriate atoms based on the type of glycosidic linkage specified (although I could be wrong on that). In fact, I just deleted all hydrogen atoms from the sugars for purposes of refinement, knowing that I could add them back in later if desired. To determine the appropriate atoms for removal from the coordinate file in order to form the desired glycosidic linkage, run the command phenix.where_mon_lib_list_cif and then look in the specified file for the type of glycosidic linkage you want. For Beta1-2, you get this: BETA1-2 . DEL-HO2 pyranose . DEL-O1 pyranose glycosidic_bond_beta1-2 This means that, in your example, > apply_cif_link { > data_link = "BETA1-2" > residue_selection_1 = chain Z and resname NAG and resid 5 > residue_selection_2 = chain Z and resname MAN and resid 4 > } you should delete the O1 atom from Man 4 of chain Z and the HO2 atom from Nag 5 of chain Z. If the PDB file contains an O1 for Man4 or an HO2 for Nag5, the refinement will fail, and I think that's the cause of the error you're receiving. If everything works as desired, the result should be that C1 of MAN will be connected to O2 of NAG, thus the 1-2 linkage. If you then load the appropriate .CIF files into Coot and/or Phenix, you should be able to refine the sugars as desired. Alpha2-6 links are not included in the mon_lib_list.cif file. If you want to refine such a linkage, my (admittedly limited) understanding is that, unfortunately, you'd have to manually create a CIF file containing the appropriate restraints - bond lengths, angles, etc. Hope you find something useful in all this. I was was ready to pull out my hair several times over the past few weeks, but now that I got it to work, it doesn't seem so bad anymore. Best of luck. Matthew --- Matthew J. Whitley, Ph.D. Postdoctoral Research Fellow Angela Gronenborn Lab Department of Structural Biology University of Pittsburgh School of Medicine On Apr 17, 2012, at 11:00 AM, phenixbb-request(a)phenix-online.org wrote: > > > Message: 6 > Date: Tue, 17 Apr 2012 11:18:57 +0100 > From: Simon Kolstoe <s.kolstoe(a)ucl.ac.uk> > To: PHENIX user mailing list <phenixbb(a)phenix-online.org> > Subject: [phenixbb] Sugar woes > Message-ID: <7BD08A7C-5B94-4448-8E8A-CBA4437E00B6(a)ucl.ac.uk> > Content-Type: text/plain; charset="us-ascii" > > Hi phenixbb, > > Every couple of years I come to build a sugar chain into a protein structure and hope the process is less painful than last time, however it seems things still are not smooth yet! > > I'm trying to build a fairly standard sugar chain onto a protein and am encountering many problems. What I am doing is using coot to get the coordinates for each sugar using the "File-> Get monomer" option and then putting the appropriate link in my phenix.refine .def file after renumbering the sugars. For example: > > apply_cif_link { > data_link = "BETA1-2" > residue_selection_1 = chain Z and resname NAG and resid 5 > residue_selection_2 = chain Z and resname MAN and resid 4 > } > apply_cif_link { > data_link = "BETA1-4" > residue_selection_1 = chain Z and resname GAL and resid 6 > residue_selection_2 = chain Z and resname NAG and resid 5 > } > > For some reason I keep getting the following error: > > --------------- > > Chain: "Z" > Number of atoms: 220 > Number of conformers: 1 > Conformer: "" > Sorry: Traceback (most recent call last): > File "/Applications/PHENIX-1.7.3-928/Contents/phenix-1.7.3-928/cctbx_project/mmtbx/monomer_library/pdb_interpretation.py", line 1042, in apply_mod > mod_mon = self.monomer.apply_mod(mod_mod_id) > File "/Applications/PHENIX-1.7.3-928/Contents/phenix-1.7.3-928/cctbx_project/mmtbx/monomer_library/cif_types.py", line 399, in apply_mod > result.delete_atom_in_place(mod_atom.atom_id) > File "/Applications/PHENIX-1.7.3-928/Contents/phenix-1.7.3-928/cctbx_project/mmtbx/monomer_library/cif_types.py", line 316, in delete_atom_in_place > raise RuntimeError("delete_atom_in_place: unknown atom_id: %s" % atom_id) > RuntimeError: delete_atom_in_place: unknown atom_id: HO2 > apply_mod failure: > pdbres="NAG Z 5 " segid="Z " > comp id: NAG-b-D > mod id: DEL-HO2 > > ------------------ > > I haven't deleted the hydrogens that came with the sugars so what I thought it was doing was trying to delete an atom that isn't there, however adding a dummy atom with the name HO2 didn't work - any ideas? > > Also it seems happy with BETA1-4 links but not ALPHA2-6 links? How do I specify this link? > > Thanks, > > Simon

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Sugar woes
by Simon Kolstoe 17 Apr '12

17 Apr '12

Hi phenixbb, Every couple of years I come to build a sugar chain into a protein structure and hope the process is less painful than last time, however it seems things still are not smooth yet! I'm trying to build a fairly standard sugar chain onto a protein and am encountering many problems. What I am doing is using coot to get the coordinates for each sugar using the "File-> Get monomer" option and then putting the appropriate link in my phenix.refine .def file after renumbering the sugars. For example: apply_cif_link { data_link = "BETA1-2" residue_selection_1 = chain Z and resname NAG and resid 5 residue_selection_2 = chain Z and resname MAN and resid 4 } apply_cif_link { data_link = "BETA1-4" residue_selection_1 = chain Z and resname GAL and resid 6 residue_selection_2 = chain Z and resname NAG and resid 5 } For some reason I keep getting the following error: --------------- Chain: "Z" Number of atoms: 220 Number of conformers: 1 Conformer: "" Sorry: Traceback (most recent call last): File "/Applications/PHENIX-1.7.3-928/Contents/phenix-1.7.3-928/cctbx_project/mmtbx/monomer_library/pdb_interpretation.py", line 1042, in apply_mod mod_mon = self.monomer.apply_mod(mod_mod_id) File "/Applications/PHENIX-1.7.3-928/Contents/phenix-1.7.3-928/cctbx_project/mmtbx/monomer_library/cif_types.py", line 399, in apply_mod result.delete_atom_in_place(mod_atom.atom_id) File "/Applications/PHENIX-1.7.3-928/Contents/phenix-1.7.3-928/cctbx_project/mmtbx/monomer_library/cif_types.py", line 316, in delete_atom_in_place raise RuntimeError("delete_atom_in_place: unknown atom_id: %s" % atom_id) RuntimeError: delete_atom_in_place: unknown atom_id: HO2 apply_mod failure: pdbres="NAG Z 5 " segid="Z " comp id: NAG-b-D mod id: DEL-HO2 ------------------ I haven't deleted the hydrogens that came with the sugars so what I thought it was doing was trying to delete an atom that isn't there, however adding a dummy atom with the name HO2 didn't work - any ideas? Also it seems happy with BETA1-4 links but not ALPHA2-6 links? How do I specify this link? Thanks, Simon

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Phaser-MR issues?
by Noinaj, Nicholas (NIH/NIDDK) [F] 15 Apr '12

15 Apr '12

Hi, I just installed the latest installer (1036) and having issues with Phaser-MR. i have a multi-domain structure (6-domains) and trying to search for the domains individually but starting with the most conserved first using the Direct search method. However, my issues are... 1- Phaser-MR appears to still be using the 'automatically determined search order' instead of the order I have selected despite me having this turned OFF 2- Phaser-MR appears to still be using the 'FAST method' despite me having DIRECT method chosen Anyone else seeing this or could i be doing something wrong here? Thanks in advance for any feedback! Cheers, Nick

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alternate conformation clashes with its symmetry mate
by Page, Rebecca 15 Apr '12

15 Apr '12

Dear phenix BB, I am having an alternate conformation clashing problem that I am having difficulty resolving: I have a protein in which the N-terminal residue is in two conformations.When the residue is in the 'A' conformation, the sidechain overlaps with the 'A' conformation sidechain density of its symmetry mate. I have modeled the occupancy at 50%. However, every time I refine, phenix pushes the 'A' conformer out of the density, likely due to clashing with its symmetry mate. Is there anyway to get around this? Thanks in advance, Rebecca

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help with validating a very low res structure
by Yunji Wu 14 Apr '12

14 Apr '12

Hi there-- Any old school experimental phasing experts want to help me out? I have an 8 angstrom structure solved using molecular replacement, refined to Rwork 0.38 and Rfree of 0.47. I also have a heavy atom (not SeMet) derivative data set to 10 angstroms. The idea is to get as much information from these data as possible so as to validate my current MR model. My approach is to calculate a difference map using the isomorphous difference Fouriers OR anomalous difference Fouriers as the amplitudes, with phases derived from the MR model-- then using the difference map to locate putative heavy atom sites. I would use various controls and experiments to (computationally) validate the credibility of these sites (e.g. cross-phasing with only iso/ano differences). Anyone have any suggestions for how to do this using Phenix? I use the GUI (generally the nightly builds), and am a newcomer to Phenix. Thanks!!

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Re: [phenixbb] on the protonation state of HIS
by Ho Leung Ng 13 Apr '12

13 Apr '12

Hi Dialing, What resolution is your structure? We are developing a method to predict hydrogen atom positions from structures of more modest resolution (out to about 1.7 A). We'd be happy to take a look at the histidines in your structure. Ho Ho Leung Ng University of Hawaii at Manoa Assistant Professor, Department of Chemistry hng(a)hawaii.edu

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Windows installer now available
by Paul Adams 13 Apr '12

13 Apr '12

Dear Colleagues, as a result of some very hard work by several members of the Phenix Team, especially Nat Echols, I'm happy to report that we now have an experimental Windows installer for Phenix available for testing in the latest nightly builds. This includes most of the Phenix components, including the GUI, and should run on Windows XP or newer. Coot and PyMOL integration is supported if these are installed. Details are available here: http://www.phenix-online.org/platforms/windows.html We encourage anyone using this to submit the automatic bug reports, or email us concerning any other problems at bugs(a)phenix-online.org. An official, fully supported Windows installer, including 64-bit version, will be available later this year. The Phenix Team -- Paul Adams Deputy Division Director, Physical Biosciences Division, 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 64, Room 248 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 64R0121 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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amazing good statistics
by Christian Roth 11 Apr '12

11 Apr '12

Dear Phenix people, is there a major improvement in the algorithm? I have refined a 2.2 Ang. room temperature dataset with very good data statistics (I think) Rmerge 3.7%(8.9%) completeness 96%(92%) I/sigI 16,6(8,8) in parentheses are the values for the highest resolution shell. After refinement I have a R/Rfree of 0.1294/0.1670. In some shells there are values close to 0.100 and in the lowest shell Rfree is lower than Rwork. The quality of the data are really quite good, what is probably one of the reasons, but I am close or below to the border of the Range of R values in the pdb. Great for me, but I wanna be sure that it is really true. It was a MolRep with a close homolog, but I run a torsion angle sim annealing to decouple R/Rfree and the MolRep was done with an poly-Ala model to prevent too much model bias. Best Regards Christian

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Unrestrained refinement and reported RMSD values
by Yuri 09 Apr '12

09 Apr '12

Hi all, I wonder if there is a way of turning off (loosening) restraints for certain residues and a ligand specifically, and will the bond/angle rmsd be printed out somewhere? Thanks -- Yuri Pompeu

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Limit Ramachandran restrain to certain region
by Nian Huang 04 Apr '12

04 Apr '12

Dear all, Is it possible to limit Ramachandran restrain to specified residues in phenix.refine? I have a couple of loops with very poor density. The refinement process always made some residues fall out of ramachandran plot no matter how I tightened the weight and adjusted the residues back. Because the diffraction is about 2.3 A, I don't want the ramachandran restrain to impact the rest of structure. Thanks. Nian Huang

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modelling a flexible peptide
by intekhab alam 04 Apr '12

04 Apr '12

Hi All I have a 3.0A dataset (SG P1211) of a protein-protein complex having mol.wt 60 and 8 Kda respectively. Molecular repalcement (60Kda protein as template) with Phaser gave a solution with 6 molecules in ASU. A continuous density is also obersved near two different chains which i consider as the second protein. I refined the density using a poly Alanine model but still i can't recognise the side chains confidently for modelling. Considering the fact that the smaller protein partner is rich in lysine, arginine, Asp and Glutamate with only 3 tyr and 4 phe, i tried to modell fragments one by one but the B-factor of the segments are quite high (in the range of 110) what will be the best strategy to improve the map for modelling. regards -- INTEKHAB ALAM LABORATORY OF STRUCTURAL BIOINFORMATICS KOREA UNIVERSITY, SEOUL

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fwd: Application deadline approaching: CCP4 summer school at APS, in USA
by Nathaniel Echols 03 Apr '12

03 Apr '12

---------- Forwarded message ---------- From: "Sanishvili, Ruslan" <rsanishvili(a)anl.gov> To: "'phenixbb(a)phenix-online.org'" <phenixbb(a)phenix-online.org> Cc: "Sanishvili, Ruslan" <rsanishvili(a)anl.gov> Date: Tue, 3 Apr 2012 17:19:36 -0500 Subject: Application deadline approaching: CCP4 summer school at APS, in USA Dear Colleagues, We would like to point out that the application deadline for the 5th annual CCP4 Summer School “From data collection to structure refinement and beyond” is April 17, 2012. The school will take place from June 19 through June 26, 2012 at the Advanced Photon Source (APS) near Chicago. There is no registration fee for the school. The students will be responsible for their own travel and lodging expenses. These and other details (The program, the list of speakers, the application process, accommodations, site access, contacts etc) can be found at the workshop website at http://www.ccp4.ac.uk/schools/APS-2012/index.php The school will cover all aspects of macromolecular structure determination and validation. Some of the world’s leading experts will be providing instruction and hand-on help. We are looking forward to another productive school this summer. Garib, Ronan and Nukri Ruslan Sanishvili (Nukri), Ph.D. GM/CA-CAT Biosciences Division, ANL 9700 S. Cass Ave. Argonne, IL 60439 Tel: (630)252-0665 Fax: (630)252-0667 rsanishvili(a)anl.gov

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Trueblood Award Nominations
by Paul Adams 03 Apr '12

03 Apr '12

Dear Colleagues, on behalf of the selection committee I'd like to draw your attention to the the Trueblood award: http://www.amercrystalassn.org/content/pages/main-award-descriptions This will next be awarded in 2013, however nominations are sought now so that the winner can be announcement this Summer. The award will be presented at the 2013 ACA meeting. Please follow this link to obtain the nomination form: http://www.amercrystalassn.org/documents/ACAnomNEW.pdf Note that the deadline for nominations is May 1st, which should be sent to marcia(a)hwi.buffalo.edu. Here is a summary of the award: Kenneth N. Trueblood Award To recognize exceptional achievement in computational or chemical crystallography. The award is established in memory of Professor Kenneth N. Trueblood, UCLA 1949-1998, who was a major force in the early use of computers and the development of crystallographic computer programs. He applied these programs to the examination of chemical and molecular details of many structures at the frontiers of research. His contribution to the famous work on vitamin B12 is one example. Professor Trueblood was a leader in the development of techniques for analysis of anisotropic motion and was also a superb teacher and a lucid author. Established in 2001, the award will be given every three years and consist of an honorarium of $1,500 and up to $1,500 in travel expenses to accept the award. -- Paul Adams Deputy Division Director, Physical Biosciences Division, 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 64, Room 248 Tel: 1-510-486-4225, Fax: 1-510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 64R0121 Berkeley, CA 94720, USA. Executive Assistant: Louise Benvenue [ LBenvenue(a)lbl.gov ][ 1-510-495-2506 ] --

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Exhaustive List of Phenix Commands
by Matthew J. Whitley 03 Apr '12

03 Apr '12

Hello all, I was wondering if somewhere, either on the web or in hardcopy, there is an exhaustive or nearly exhaustive list of Phenix commands. For example, from a Phenix BB thread earlier in the day I learned of the existence of the phenix.r_factor_statistics command for gaining insight into where your R/Rfree values place you in regard to structures of similar resolution. As I read more of the messages posted to the Phenix BB, I become aware of more and more nifty things that Phenix can do that I simply was not aware of, and I was wondering if some kind of master list of Phenix commands is available somewhere. Thanks to all the developers for making this amazing program available to the x-ray community. Thanks, Matthew --- Matthew J. Whitley, Ph.D. Postdoctoral Research Fellow Angela Gronenborn Lab Department of Structural Biology University of Pittsburgh School of Medicine

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amazing good statistics add
by Christian Roth 03 Apr '12

03 Apr '12

In general the Rvalues of course fit very well Rmerge. A good sign that it should be fine, as far as I remember correctly about the theoretical limits for the Rvalues after refinement compared to the experiment. Best Regards Christian

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Creating dictionary restraints for a LINK
by Mario Sanches 03 Apr '12

03 Apr '12

I have a question regarding link dictionary generation. Nigel helped me with a molecule dictionary last week (thank you Nigel) so the molecule is refining well now. This molecule is covalently bound to on of the residues. I tried generating a dictionary that describes both the molecule and the link but so far phenix.refine is ignoring it. Again, the molecule itself refines very well but the link is not there. What is the best way to define it? Thank you very much. -- Mario Sanches Postdoctoral Researcher Samuel Lunenfeld Research Institute Mount Sinai Hospital 600 University Ave Toronto - Ontario Canada M5G 1X5 http://ca.linkedin.com/in/mariosanches

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DEN refinement is crashing
by Mario Sanches 02 Apr '12

02 Apr '12

I am running phenix.refine using the graphical interface. Under "global refinement paramerters..." I am selecting "DEN". The problem is that Python crashes all the time, always at the same point (see portion of the log output below). Is it a known bug? Is DEN incompatible with some of the options in refinement? My resolution is 2.9A by the way. Thank you for your inputs. Mario Sanches ___________________________ Log output final portion: tardy dynamics: number of bodies: 3678 number of degrees of freedom: 3713 number of atoms * 3: 38220 ratio: 0.097 = 1/10.29 temperature degrees of freedom: cartesian (38220) kinetic energy sensitivity to generalized velocities: n: 3713 min: 3.61771e-06 max: 0.0300001 mean: 0.00410663 time step: 0.00100 pico seconds velocity scaling: True suppressing allowed origin shifts: False new target temperature: 2500.00 K step= 1 temperature= 2500.0 rmsd=0.0446 r_work=0.3010 r_free=0.3214 -- Mario Sanches Postdoctoral Researcher Samuel Lunenfeld Research Institute Mount Sinai Hospital 600 University Ave Toronto - Ontario Canada M5G 1X5 http://ca.linkedin.com/in/mariosanches

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labelit.index is too precise not to allow 0.000001 deg difference
by fukamitka＠chugai-pharm.co.jp 02 Apr '12

02 Apr '12

Dear Phenix developers, I had a problem in indexing by labelit.index in phenix-1.7.3-928, getting the error below: InputFileError: Input error: All images must have same oscillation range (delta phi). My dataset was collected by inhouse R-axis with 0.8 deg oscillation. Image header values of oscillation range fluctuate between 0.799999 - 0.800004 degrees. When I specified two images whose delta phi angles were different, say 0.799999 and 0.800003, labelit.index stopped with the error above. I don't think a goniometer have such a precision, therefore I think line 249 in /phenix-1.7.3-928/labelit/command_line/imagefiles.py should be modified not to use == instead of similar_delta_phi() or something. 246 if False in [similar_wavelength(self.images[0],self.images[x]) for x in xrange(1,Nimages)]: 247 raise InputFileError("""All images must have similar wavelength.""") 248 249 if False in [self.images[0].deltaphi==self.images[x].deltaphi for x in xrange(1,Nimages)]: 250 raise InputFileError("""All images must have same oscillation range (delta phi).""") Best regards, Takaaki Fukami ----- Dr. Takaaki Fukami (mailto:[email protected]) Discovery Research Dept. (Biostructure Gr.) Roche Group: Chugai Pharmaceutical Co.,Ltd.

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very informative - Trends in Data Fabrication
by Bosch, Juergen 31 Mar '12

31 Mar '12

really fascinating, bringing back the discussion for a repository for your collected frames. Jürgen Acta Cryst. (2012). F68, 366-376 doi:10.1107/S1744309112008421<http://dx.doi.org/10.1107/S1744309112008421> Detection and analysis of unusual features in the structural model and structure-factor data of a birch pollen allergen B. Rupp<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Rupp,%20B.> Abstract: Physically improbable features in the model of the birch pollen structure Bet v 1d (PDB entry 3k78<http://pdb.pdb.bnl.gov/pdb-bin/opdbshort?3k78>) are faithfully reproduced in electron density generated with the deposited structure factors, but these structure factors themselves exhibit properties that are characteristic of data calculated from a simple model and are inconsistent with the data and error model obtained through experimental measurements. The refinement of the 3k78<http://pdb.pdb.bnl.gov/pdb-bin/opdbshort?3k78>model against these structure factors leads to an isomorphous structure different from the deposited model with an implausibly small R value (0.019). The abnormal refinement is compared with normal refinement of an isomorphous variant structure of Bet v 1l (PDB entry 1fm4<http://pdb.pdb.bnl.gov/pdb-bin/opdbshort?1fm4>). A variety of analytical tools, including the application of Diederichs plots, R plots and bulk-solvent analysis are discussed as promising aids in validation. The examination of the Bet v 1d structure also cautions against the practice of indicating poorly defined protein chain residues through zero occupancies. The recommendation to preserve diffraction images is amplified. ...................... Jürgen Bosch Johns Hopkins University Bloomberg School of Public Health Department of Biochemistry & Molecular Biology Johns Hopkins Malaria Research Institute 615 North Wolfe Street, W8708 Baltimore, MD 21205 Office: +1-410-614-4742 Lab: +1-410-614-4894 Fax: +1-410-955-2926 http://web.mac.com/bosch_lab/

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Problems fitting NADH
by Phillip Steindel 30 Mar '12

30 Mar '12

Dear all, I'm trying to fit a NADH into a 1.7 Å structure. LigandFit worked with just the three-letter code (NAI), however phenix.refine won't work with just the model. If I use eLBOW to create restraints, meanwhile, the ligand gets distorted during refinement (non-tetrahedral phosphates, mainly). I'm not sure exactly how I'm supposed to be generating these restraints- any help is appreciated. Thank you, Phillip Steindel Theobald Lab Department of Biochemistry Brandeis University

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Re: [phenixbb] [ccp4bb] a small trick for protein and organic compound cocrystallization.
by Bryan Lepore 30 Mar '12

30 Mar '12

On Fri, Mar 30, 2012 at 3:26 PM, Jacob Keller <j-keller2(a)fsm.northwestern.edu> wrote: > What's the harm? have you seen usenet/Google groups? -Bryan

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a small trick for protein and organic compound cocrystallization.
by Kevin Jin 30 Mar '12

30 Mar '12

Dear All, Here is way I have used for protein and hydrophobic organic compound cocrystallization. Via this method, less amount of DMSO will be used to aviod protein ppt. I hope you can use for your research. http://www.jinkai.org/Xtal.html Regards, -- Kevin Jin Sharing knowledge each other is always very joyful...... Website: http://www.jinkai.org/

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