3v88: Difference between revisions
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==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]] 2.30Å' 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]] 2.3Å</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=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. | |||
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 3v88" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Belmonte | [[Category: Belmonte L]] | ||
[[Category: Nicolini | [[Category: Nicolini C]] | ||
[[Category: Pechkova | [[Category: Pechkova E]] | ||
[[Category: Scudieri | [[Category: Scudieri D]] | ||
[[Category: Tripathi | [[Category: Tripathi S]] | ||
Latest revision as of 09:15, 17 October 2024
Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Best Case)Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Best Case)
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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