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4c3c
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Thaumatin refined against hatrx data for time-point 1== | |
| + | <StructureSection load='4c3c' size='340' side='right'caption='[[4c3c]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4c3c]] 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=4C3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3C 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3c OCA], [https://pdbe.org/4c3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3c RCSB], [https://www.ebi.ac.uk/pdbsum/4c3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3c 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 == | ||
| + | We describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy. | ||
| - | + | Time-resolved crystallography using the Hadamard transform.,Yorke BA, Beddard GS, Owen RL, Pearson AR Nat Methods. 2014 Nov;11(11):1131-4. doi: 10.1038/nmeth.3139. Epub 2014 Oct 5. PMID:25282611<ref>PMID:25282611</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4c3c" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thaumatococcus daniellii]] | ||
| + | [[Category: Beddard GS]] | ||
| + | [[Category: Owen RL]] | ||
| + | [[Category: Pearson AR]] | ||
| + | [[Category: Yorke BA]] | ||
Current revision
Thaumatin refined against hatrx data for time-point 1
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