7ays: Difference between revisions
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==Structure of bovine trypsin determined from single femtosecond snapshots per orientation at room temperature== | ==Structure of bovine trypsin determined from single femtosecond snapshots per orientation at room temperature== | ||
<StructureSection load='7ays' size='340' side='right'caption='[[7ays]]' scene=''> | <StructureSection load='7ays' size='340' side='right'caption='[[7ays]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AYS OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[7ays]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AYS FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </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=7ays FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ays OCA], [https://pdbe.org/7ays PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ays RCSB], [https://www.ebi.ac.uk/pdbsum/7ays PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ays ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation is based on the shape of the Wilson plot, cumulative intensity distribution compared with theoretical distribution, I/sigma, Rmerge/Rmeas and CC1/2 statistics versus resolution. The FemtoMAX beamline provides an interesting alternative to X-ray free-electron lasers when studying reversible processes in protein crystals. | |||
High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection.,Jensen M, Ahlberg Gagner V, Cabello Sanchez J, Bengtsson AUJ, Ekstrom JC, Bjorg Ulfarsdottir T, Garcia-Bonete MJ, Jurgilaitis A, Kroon D, Pham VT, Checcia S, Coudert-Alteirac H, Schewa S, Rossle M, Rodilla H, Stake J, Zhaunerchyk V, Larsson J, Katona G J Synchrotron Radiat. 2021 Jan 1;28(Pt 1):64-70. doi: 10.1107/S1600577520014599. , Epub 2021 Jan 1. PMID:33399553<ref>PMID:33399553</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ays" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jensen M]] | [[Category: Trypsin]] | ||
[[Category: Jensen, M]] | |||
[[Category: Hydrolase]] | |||
[[Category: Serine protease]] | |||
Revision as of 13:30, 4 August 2021
Structure of bovine trypsin determined from single femtosecond snapshots per orientation at room temperatureStructure of bovine trypsin determined from single femtosecond snapshots per orientation at room temperature
Structural highlights
Publication Abstract from PubMedProtein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation is based on the shape of the Wilson plot, cumulative intensity distribution compared with theoretical distribution, I/sigma, Rmerge/Rmeas and CC1/2 statistics versus resolution. The FemtoMAX beamline provides an interesting alternative to X-ray free-electron lasers when studying reversible processes in protein crystals. High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection.,Jensen M, Ahlberg Gagner V, Cabello Sanchez J, Bengtsson AUJ, Ekstrom JC, Bjorg Ulfarsdottir T, Garcia-Bonete MJ, Jurgilaitis A, Kroon D, Pham VT, Checcia S, Coudert-Alteirac H, Schewa S, Rossle M, Rodilla H, Stake J, Zhaunerchyk V, Larsson J, Katona G J Synchrotron Radiat. 2021 Jan 1;28(Pt 1):64-70. doi: 10.1107/S1600577520014599. , Epub 2021 Jan 1. PMID:33399553[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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