6ybx: Difference between revisions

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<StructureSection load='6ybx' size='340' side='right'caption='[[6ybx]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
<StructureSection load='6ybx' size='340' side='right'caption='[[6ybx]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ybx]] 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=6YBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YBX FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YBX 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]] 1.14&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=6ybx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ybx OCA], [https://pdbe.org/6ybx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ybx RCSB], [https://www.ebi.ac.uk/pdbsum/6ybx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ybx ProSAT]</span></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=6ybx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ybx OCA], [https://pdbe.org/6ybx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ybx RCSB], [https://www.ebi.ac.uk/pdbsum/6ybx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ybx ProSAT]</span></td></tr>
</table>
</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 ==
Sample handling and manipulation for cryoprotection currently remain critical factors in X-ray structural determination. While several microchips for macromolecular crystallization have been proposed during the last two decades to partially overcome crystal-manipulation issues, increased background noise originating from the scattering of chip-fabrication materials has so far limited the attainable resolution of diffraction data. Here, the conception and use of low-cost, X-ray-transparent microchips for in situ crystallization and direct data collection, and structure determination at atomic resolution close to 1.0 A, is presented. The chips are fabricated by a combination of either OSTEMER and Kapton or OSTEMER and Mylar materials for the implementation of counter-diffusion crystallization experiments. Both materials produce a sufficiently low scattering background to permit atomic resolution diffraction data collection at room temperature and the generation of 3D structural models of the tested model proteins lysozyme, thaumatin and glucose isomerase. Although the high symmetry of the three model protein crystals produced almost complete data sets at high resolution, the potential of in-line data merging and scaling of the multiple crystals grown along the microfluidic channels is also presented and discussed.
Attaining atomic resolution from in situ data collection at room temperature using counter-diffusion-based low-cost microchips.,Gavira JA, Rodriguez-Ruiz I, Martinez-Rodriguez S, Basu S, Teychene S, McCarthy AA, Mueller-Dieckman C Acta Crystallogr D Struct Biol. 2020 Aug 1;76(Pt 8):751-758. doi:, 10.1107/S2059798320008475. Epub 2020 Jul 27. PMID:32744257<ref>PMID:32744257</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ybx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Gavira JA]]
[[Category: Gavira JA]]
[[Category: Martinez-Rodriguez S]]
[[Category: Martinez-Rodriguez S]]

Latest revision as of 10:44, 23 October 2024

RT structure of Thaumatin obtained at 1.14 A resolution from crystal grown in a Mylar microchip.

6ybx, resolution 1.14Å

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