6s1g: Difference between revisions
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==Structure of thaumatin determined at SwissFEL using native-SAD at 6.06 keV from 50,000 diffraction patterns | ==Structure of thaumatin determined at SwissFEL using native-SAD at 6.06 keV from 50,000 diffraction patterns== | ||
<StructureSection load='6s1g' size='340' side='right'caption='[[6s1g]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6s1g' size='340' side='right'caption='[[6s1g]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S1G FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6s1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s1g OCA], [https://pdbe.org/6s1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s1g RCSB], [https://www.ebi.ac.uk/pdbsum/6s1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s1g ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6s1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s1g OCA], [https://pdbe.org/6s1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s1g RCSB], [https://www.ebi.ac.uk/pdbsum/6s1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s1g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Abela R]] | [[Category: Abela R]] | ||
[[Category: Basu S]] | [[Category: Basu S]] | ||
Latest revision as of 16:05, 6 November 2024
Structure of thaumatin determined at SwissFEL using native-SAD at 6.06 keV from 50,000 diffraction patternsStructure of thaumatin determined at SwissFEL using native-SAD at 6.06 keV from 50,000 diffraction patterns
Structural highlights
Publication Abstract from PubMedLong-wavelength pulses from the Swiss X-ray free-electron laser (XFEL) have been used for de novo protein structure determination by native single-wavelength anomalous diffraction (native-SAD) phasing of serial femtosecond crystallography (SFX) data. In this work, sensitive anomalous data-quality indicators and model proteins were used to quantify improvements in native-SAD at XFELs such as utilization of longer wavelengths, careful experimental geometry optimization, and better post-refinement and partiality correction. Compared with studies using shorter wavelengths at other XFELs and older software versions, up to one order of magnitude reduction in the required number of indexed images for native-SAD was achieved, hence lowering sample consumption and beam-time requirements significantly. Improved data quality and higher anomalous signal facilitate so-far underutilized de novo structure determination of challenging proteins at XFELs. Improvements presented in this work can be used in other types of SFX experiments that require accurate measurements of weak signals, for example time-resolved studies. Advances in long-wavelength native phasing at X-ray free-electron lasers.,Nass K, Cheng R, Vera L, Mozzanica A, Redford S, Ozerov D, Basu S, James D, Knopp G, Cirelli C, Martiel I, Casadei C, Weinert T, Nogly P, Skopintsev P, Usov I, Leonarski F, Geng T, Rappas M, Dore AS, Cooke R, Nasrollahi Shirazi S, Dworkowski F, Sharpe M, Olieric N, Bacellar C, Bohinc R, Steinmetz MO, Schertler G, Abela R, Patthey L, Schmitt B, Hennig M, Standfuss J, Wang M, Milne CJ IUCrJ. 2020 Sep 9;7(Pt 6):965-975. doi: 10.1107/S2052252520011379. eCollection, 2020 Nov 1. PMID:33209311[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Large Structures
- Abela R
- Basu S
- Casadei C
- Cheng R
- Cirelli C
- Cooke R
- Dore AS
- Dworkowski F
- Geng T
- Hennig M
- James D
- Knopp G
- Leonarski F
- Martiel I
- Milne JC
- Mozzanica A
- Nasrollahi Shirazi S
- Nass K
- Nogly P
- Olieric N
- Ozerov D
- Patthey L
- Rappas M
- Redford S
- Schertler G
- Schmitt B
- Sharpe M
- Skopintsev P
- Standfuss J
- Steinmetz MO
- Usov I
- Vera L
- Wang M
- Weinert T