8awd: Difference between revisions
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The | ==Xylose Isomerase in 95% relative humidity environment== | ||
<StructureSection load='8awd' size='340' side='right'caption='[[8awd]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8awd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AWD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8awd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8awd OCA], [https://pdbe.org/8awd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8awd RCSB], [https://www.ebi.ac.uk/pdbsum/8awd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8awd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/XYLA_STRRU XYLA_STRRU] Involved in D-xylose catabolism. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We introduce the spitrobot, a protein crystal plunger, enabling reaction quenching via cryo-trapping with a time-resolution in the millisecond range. Protein crystals are mounted on canonical micromeshes on an electropneumatic piston, where the crystals are kept in a humidity and temperature-controlled environment, then reactions are initiated via the liquid application method (LAMA) and plunging into liquid nitrogen is initiated after an electronically set delay time to cryo-trap intermediate states. High-magnification images are automatically recorded before and after droplet deposition, prior to plunging. The SPINE-standard sample holder is directly plunged into a storage puck, enabling compatibility with high-throughput infrastructure. Here we demonstrate binding of glucose and 2,3-butanediol in microcrystals of xylose isomerase, and of avibactam and ampicillin in microcrystals of the extended spectrum beta-lactamase CTX-M-14. We also trap reaction intermediates and conformational changes in macroscopic crystals of tryptophan synthase to demonstrate that the spitrobot enables insight into catalytic events. | |||
Millisecond cryo-trapping by the spitrobot crystal plunger simplifies time-resolved crystallography.,Mehrabi P, Sung S, von Stetten D, Prester A, Hatton CE, Kleine-Dopke S, Berkes A, Gore G, Leimkohl JP, Schikora H, Kollewe M, Rohde H, Wilmanns M, Tellkamp F, Schulz EC Nat Commun. 2023 Apr 25;14(1):2365. doi: 10.1038/s41467-023-37834-w. PMID:37185266<ref>PMID:37185266</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8awd" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Kleine-Doepke | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Leimkohl | [[Category: Streptomyces rubiginosus]] | ||
[[Category: | [[Category: Berkes A]] | ||
[[Category: Prester | [[Category: Gore G]] | ||
[[Category: | [[Category: Hatton CE]] | ||
[[Category: | [[Category: Kleine-Doepke S]] | ||
[[Category: | [[Category: Kollewe M]] | ||
[[Category: | [[Category: Leimkohl JP]] | ||
[[Category: | [[Category: Mehrabi P]] | ||
[[Category: | [[Category: Prester A]] | ||
[[Category: Rohde H]] | |||
[[Category: Schikora H]] | |||
[[Category: Schulz EC]] | |||
[[Category: Sung S]] | |||
[[Category: Tellkamp F]] | |||
[[Category: Wilmanns M]] | |||
[[Category: Von Stetten D]] | |||
Revision as of 07:01, 25 May 2023
Xylose Isomerase in 95% relative humidity environmentXylose Isomerase in 95% relative humidity environment
Structural highlights
FunctionXYLA_STRRU Involved in D-xylose catabolism. Publication Abstract from PubMedWe introduce the spitrobot, a protein crystal plunger, enabling reaction quenching via cryo-trapping with a time-resolution in the millisecond range. Protein crystals are mounted on canonical micromeshes on an electropneumatic piston, where the crystals are kept in a humidity and temperature-controlled environment, then reactions are initiated via the liquid application method (LAMA) and plunging into liquid nitrogen is initiated after an electronically set delay time to cryo-trap intermediate states. High-magnification images are automatically recorded before and after droplet deposition, prior to plunging. The SPINE-standard sample holder is directly plunged into a storage puck, enabling compatibility with high-throughput infrastructure. Here we demonstrate binding of glucose and 2,3-butanediol in microcrystals of xylose isomerase, and of avibactam and ampicillin in microcrystals of the extended spectrum beta-lactamase CTX-M-14. We also trap reaction intermediates and conformational changes in macroscopic crystals of tryptophan synthase to demonstrate that the spitrobot enables insight into catalytic events. Millisecond cryo-trapping by the spitrobot crystal plunger simplifies time-resolved crystallography.,Mehrabi P, Sung S, von Stetten D, Prester A, Hatton CE, Kleine-Dopke S, Berkes A, Gore G, Leimkohl JP, Schikora H, Kollewe M, Rohde H, Wilmanns M, Tellkamp F, Schulz EC Nat Commun. 2023 Apr 25;14(1):2365. doi: 10.1038/s41467-023-37834-w. PMID:37185266[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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