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==Crystal structure of Bovine Pancreatic Trypsin in complex with Benzamidine at Room Temperature== | ==Crystal structure of Bovine Pancreatic Trypsin in complex with Benzamidine at Room Temperature== | ||
<StructureSection load='7wa0' size='340' side='right'caption='[[7wa0]]' scene=''> | <StructureSection load='7wa0' size='340' side='right'caption='[[7wa0]], [[Resolution|resolution]] 1.77Å' 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=7WA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WA0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7wa0]] 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=7WA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WA0 FirstGlance]. <br> | ||
</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=7wa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wa0 OCA], [https://pdbe.org/7wa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wa0 RCSB], [https://www.ebi.ac.uk/pdbsum/7wa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wa0 ProSAT]</span></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]] 1.77Å</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=DMS:DIMETHYL+SULFOXIDE'>DMS</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=7wa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wa0 OCA], [https://pdbe.org/7wa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wa0 RCSB], [https://www.ebi.ac.uk/pdbsum/7wa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wa0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In situ diffraction data collection using crystallization plates has been utilized for macromolecules to evaluate crystal quality without requiring additional sample treatment such as cryocooling. Although it is difficult to collect complete data sets using this technique due to the mechanical limitation of crystal rotation, recent advances in methods for data collection from multiple crystals have overcome this issue. At SPring-8, an in situ diffraction measurement system was constructed consisting of a goniometer for a plate, an articulated robot and plate storage. Using this system, complete data sets were obtained utilizing the small-wedge measurement method. Combining this system with an acoustic liquid handler to prepare protein-ligand complex crystals by applying fragment compounds to trypsin crystals for in situ soaking, binding was confirmed for seven out of eight compounds. These results show that the system functioned properly to collect complete data for structural analysis and to expand the capability for ligand screening in combination with a liquid dispenser. | |||
In situ crystal data-collection and ligand-screening system at SPring-8.,Okumura H, Sakai N, Murakami H, Mizuno N, Nakamura Y, Ueno G, Masunaga T, Kawamura T, Baba S, Hasegawa K, Yamamoto M, Kumasaka T Acta Crystallogr F Struct Biol Commun. 2022 Jun 1;78(Pt 6):241-251. doi:, 10.1107/S2053230X22005283. Epub 2022 May 27. PMID:35647681<ref>PMID:35647681</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7wa0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kumasaka T]] | [[Category: Kumasaka T]] | ||
Revision as of 20:38, 29 November 2023
Crystal structure of Bovine Pancreatic Trypsin in complex with Benzamidine at Room TemperatureCrystal structure of Bovine Pancreatic Trypsin in complex with Benzamidine at Room Temperature
Structural highlights
FunctionPublication Abstract from PubMedIn situ diffraction data collection using crystallization plates has been utilized for macromolecules to evaluate crystal quality without requiring additional sample treatment such as cryocooling. Although it is difficult to collect complete data sets using this technique due to the mechanical limitation of crystal rotation, recent advances in methods for data collection from multiple crystals have overcome this issue. At SPring-8, an in situ diffraction measurement system was constructed consisting of a goniometer for a plate, an articulated robot and plate storage. Using this system, complete data sets were obtained utilizing the small-wedge measurement method. Combining this system with an acoustic liquid handler to prepare protein-ligand complex crystals by applying fragment compounds to trypsin crystals for in situ soaking, binding was confirmed for seven out of eight compounds. These results show that the system functioned properly to collect complete data for structural analysis and to expand the capability for ligand screening in combination with a liquid dispenser. In situ crystal data-collection and ligand-screening system at SPring-8.,Okumura H, Sakai N, Murakami H, Mizuno N, Nakamura Y, Ueno G, Masunaga T, Kawamura T, Baba S, Hasegawa K, Yamamoto M, Kumasaka T Acta Crystallogr F Struct Biol Commun. 2022 Jun 1;78(Pt 6):241-251. doi:, 10.1107/S2053230X22005283. Epub 2022 May 27. PMID:35647681[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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