7wb8: Difference between revisions
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==Crystal structure of Bovine Pancreatic Trypsin in complex with 5-Methoxytryptamine at Room Temperature== | |||
<StructureSection load='7wb8' size='340' side='right'caption='[[7wb8]], [[Resolution|resolution]] 1.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7wb8]] 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=7WB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WB8 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]] 1.38Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=F5U:2-(5-methoxy-1~{H}-indol-3-yl)ethanamine'>F5U</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=7wb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wb8 OCA], [https://pdbe.org/7wb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7wb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wb8 ProSAT]</span></td></tr> | |||
</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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7wb8" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Sakai | ==See Also== | ||
[[Category: | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Kumasaka T]] | |||
[[Category: Okumura H]] | |||
[[Category: Sakai N]] | |||
[[Category: Yamamoto M]] | |||
Latest revision as of 09:53, 21 November 2024
Crystal structure of Bovine Pancreatic Trypsin in complex with 5-Methoxytryptamine at Room TemperatureCrystal structure of Bovine Pancreatic Trypsin in complex with 5-Methoxytryptamine 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. See AlsoReferences
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