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==The 0.90 angstrom structure (I222) of glucose isomerase crystallized in high-strength agarose hydrogel== | ==The 0.90 angstrom structure (I222) of glucose isomerase crystallized in high-strength agarose hydrogel== | ||
<StructureSection load='5avh' size='340' side='right' caption='[[5avh]], [[Resolution|resolution]] 0.90Å' scene=''> | <StructureSection load='5avh' size='340' side='right'caption='[[5avh]], [[Resolution|resolution]] 0.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5avh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AVH FirstGlance]. <br> | <table><tr><td colspan='2'>[[5avh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_rubiginosus"_preobrazhenskaya_et_al._in_gauze_et_al._1957 "actinomyces rubiginosus" preobrazhenskaya et al. in gauze et al. 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AVH FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5avd|5avd]], [[5avg|5avg]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5avd|5avd]], [[5avg|5avg]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xylA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1929 "Actinomyces rubiginosus" Preobrazhenskaya et al. in Gauze et al. 1957])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5avh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avh OCA], [http://pdbe.org/5avh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5avh RCSB], [http://www.ebi.ac.uk/pdbsum/5avh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5avh ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5avh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avh OCA], [http://pdbe.org/5avh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5avh RCSB], [http://www.ebi.ac.uk/pdbsum/5avh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5avh ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Actinomyces rubiginosus preobrazhenskaya et al. in gauze et al. 1957]] | |||
[[Category: Large Structures]] | |||
[[Category: Xylose isomerase]] | [[Category: Xylose isomerase]] | ||
[[Category: Adachi, H]] | [[Category: Adachi, H]] | ||
Revision as of 10:32, 3 July 2019
The 0.90 angstrom structure (I222) of glucose isomerase crystallized in high-strength agarose hydrogelThe 0.90 angstrom structure (I222) of glucose isomerase crystallized in high-strength agarose hydrogel
Structural highlights
Function[XYLA_STRRU] Involved in D-xylose catabolism. Publication Abstract from PubMedHigh-throughput protein X-ray crystallography offers a significant opportunity to facilitate drug discovery. The most reliable approach is to determine the three-dimensional structure of the protein-ligand complex by soaking the ligand in apo crystals. However, protein apo crystals produced by conventional crystallization in a solution are fatally damaged by osmotic shock during soaking. To overcome this difficulty, we present a novel technique for growing protein crystals in a high-concentration hydrogel that is completely gellified and exhibits high strength. This technique allowed us essentially to increase the mechanical stability of the crystals, preventing serious damage to the crystals caused by osmotic shock. Thus, this method may accelerate structure-based drug discoveries. Growth of protein crystals in hydrogels prevents osmotic shock.,Sugiyama S, Maruyama M, Sazaki G, Hirose M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Matsumura H J Am Chem Soc. 2012 Apr 4;134(13):5786-9. doi: 10.1021/ja301584y. Epub 2012 Mar, 27. PMID:22435400[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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