3v88: Difference between revisions

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-'''Unreleased structure'''
-The entry 3v88 is ON HOLD  until Paper Publication
+==Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Best Case)==
+<StructureSection load='3v88' size='340' side='right'caption='[[3v88]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3v88]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V88 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]] 2.3&#8491;</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></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=3v88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v88 OCA], [https://pdbe.org/3v88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v88 RCSB], [https://www.ebi.ac.uk/pdbsum/3v88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v88 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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 ==
+A state-of-the-art review of the role of the Langmuir-Blodgett nanotemplate on protein crystal structures is here presented. Crystals grown by nanostructured template appear more radiation resistant than the classical ones, even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The electron density maps and the changes in parameters such as total diffractive power, B-factor, and pairwise R-factor have been discussed. Protein crystals, grown by the Langmuir-Blodgett nanotemplate-based method, proved to be more radiation resistant compared to crystals grown by the classical hanging drop method in terms of both global and specific damage.
-Authors: Belmonte, L., Scudieri, D., Tripathi, S., Pechkova, E., Nicolini, C.
+Langmuir-blodgett nanotemplate and radiation resistance in protein crystals: state of the art.,Belmonte L, Pechkova E, Tripathi S, Scudieri D, Nicolini C Crit Rev Eukaryot Gene Expr. 2012;22(3):219-32. PMID:23140163<ref>PMID:23140163</ref>
-Description: Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Best Case)
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3v88" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Thaumatococcus daniellii]]
+[[Category: Belmonte L]]
+[[Category: Nicolini C]]
+[[Category: Pechkova E]]
+[[Category: Scudieri D]]
+[[Category: Tripathi S]]