5avg: Difference between revisions

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-'''Unreleased structure'''
+==The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel==
+<StructureSection load='5avg' size='340' side='right' caption='[[5avg]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5avg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AVG FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5avd|5avd]], [[5avh|5avh]]</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=5avg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5avg RCSB], [http://www.ebi.ac.uk/pdbsum/5avg PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/THM1_THADA THM1_THADA]] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
+<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.
-The entry 5avg is ON HOLD
+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>
-Authors: Sugiyama, S., Shimizu, N., Maruyama, M., Sazaki, G., Hirose, M., Adachi, H., Takano, K., Murakami, S., Inoue, T., Mori, Y., Matsumura, H.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Thaumatococcus daniellii]]
+[[Category: Adachi, H]]
+[[Category: Hirose, M]]
 [[Category: Inoue, T]]
-[[Category: Hirose, M]]
+[[Category: Maruyama, M]]
-[[Category: Takano, K]]
+[[Category: Matsumura, H]]
 [[Category: Mori, Y]]
-[[Category: Matsumura, H]]
+[[Category: Murakami, S]]
+[[Category: Sazaki, G]]
 [[Category: Shimizu, N]]
-[[Category: Murakami, S]]
 [[Category: Sugiyama, S]]
-[[Category: Sazaki, G]]
+[[Category: Takano, K]]
-[[Category: Maruyama, M]]
+[[Category: High-strength agarose]]
-[[Category: Adachi, H]]
+[[Category: Hydrogel]]
+[[Category: Plant protein]]
+[[Category: Thaumatin]]