6coa: Difference between revisions
m Protected "6coa" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==1.2 A Structure of Thaumatin Crystallized in Gel== | |||
<StructureSection load='6coa' size='340' side='right' caption='[[6coa]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6coa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kwn 1kwn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6COA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6COA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1thw|1thw]], [[1thv|1thv]], [[1thu|1thu]]</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=6coa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6coa OCA], [http://pdbe.org/6coa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6coa RCSB], [http://www.ebi.ac.uk/pdbsum/6coa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6coa ProSAT]</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 == | |||
One reason for introducing a gel in the crystallization medium of proteins is its ability to reduce convection in solution. This can lead to better nucleation and growth conditions, and to crystals having enhanced diffraction properties. We report here the X-ray characterization at room temperature of high-quality crystals of the intensely sweet thaumatin prepared in a sodium tartrate solution gelified with 0.15% (m/v) agarose. Using a synchrotron radiation, these crystals diffracted to a previously unachieved resolution. A diffraction dataset was collected from four crystals at a resolution of 1.2 A with a R(sym) of 3.6% and a completeness of 99%. Refinement was carried out to a final crystallographic R-factor of 12.0%. The quality of the electron density map allowed for the observation of fine structural details in the protein and its solvation shell. Crystallization in gel might be used more generally to improve the quality of macromolecular crystals. Advantages provided by the gelified medium in the frame of structural studies are emphasized. | |||
Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature.,Sauter C, Lorber B, Giege R Proteins. 2002 Aug 1;48(2):146-50. PMID:12112683<ref>PMID:12112683</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6coa" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Thaumatococcus daniellii]] | |||
[[Category: Brzezinski, D]] | [[Category: Brzezinski, D]] | ||
[[Category: Giege, R]] | [[Category: Giege, R]] | ||
[[Category: | [[Category: Lorber, B]] | ||
[[Category: Porebski, P J]] | |||
[[Category: Sauter, C]] | [[Category: Sauter, C]] | ||
[[Category: | [[Category: Shabalin, I G]] | ||
[[Category: Agarose gel]] | |||
[[Category: Apcf]] | |||
[[Category: Microgravity]] | |||
[[Category: Plant protein]] | |||
[[Category: Sweet tasting protein]] | |||