3v8a
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Worst Case)== | |
| + | <StructureSection load='3v8a' size='340' side='right'caption='[[3v8a]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3v8a]] 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=3V8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V8A 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]] 2.3Å</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=3v8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v8a OCA], [https://pdbe.org/3v8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v8a RCSB], [https://www.ebi.ac.uk/pdbsum/3v8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v8a 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3v8a" 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]] | ||
Current revision
Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Worst Case)
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