5avh: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[5avh]] 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=5AVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AVH 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=5avh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avh OCA], [https://pdbe.org/5avh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5avh RCSB], [https://www.ebi.ac.uk/pdbsum/5avh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5avh 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]] 0.9&#8491;</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=5avh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avh OCA], [https://pdbe.org/5avh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5avh RCSB], [https://www.ebi.ac.uk/pdbsum/5avh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5avh 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 ==
-High-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<ref>PMID:22435400</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5avh" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>