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5lh1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Low dose Thaumatin - 360-400 ms.== | |
| + | <StructureSection load='5lh1' size='340' side='right'caption='[[5lh1]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lh1]] 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=5LH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LH1 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]] 1.9Å</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=5lh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lh1 OCA], [https://pdbe.org/5lh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lh1 RCSB], [https://www.ebi.ac.uk/pdbsum/5lh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lh1 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 == | ||
| + | Many biochemical processes take place on timescales ranging from femto-seconds to seconds. Accordingly, any time-resolved experiment must be matched to the speed of the structural changes of interest. Therefore, the timescale of interest defines the requirements of the X-ray source, instrumentation and data-collection strategy. In this study, a minimalistic approach for in situ crystallization is presented that requires only a few microlitres of sample solution containing a few hundred crystals. It is demonstrated that complete diffraction data sets, merged from multiple crystals, can be recorded within only a few minutes of beamtime and allow high-resolution structural information of high quality to be obtained with a temporal resolution of 40 ms. Global and site-specific radiation damage can be avoided by limiting the maximal dose per crystal to 400 kGy. Moreover, analysis of the data collected at higher doses allows the time-resolved observation of site-specific radiation damage. Therefore, our approach is well suited to observe structural changes and possibly enzymatic reactions in the low-millisecond regime. | ||
| - | + | A multicrystal diffraction data-collection approach for studying structural dynamics with millisecond temporal resolution.,Schubert R, Kapis S, Gicquel Y, Bourenkov G, Schneider TR, Heymann M, Betzel C, Perbandt M IUCrJ. 2016 Oct 26;3(Pt 6):393-401. eCollection 2016 Nov 1. PMID:27840678<ref>PMID:27840678</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lh1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thaumatococcus daniellii]] | ||
| + | [[Category: Betzel C]] | ||
| + | [[Category: Bourenkov G]] | ||
| + | [[Category: Giquel Y]] | ||
| + | [[Category: Heymann M]] | ||
| + | [[Category: Kapis S]] | ||
| + | [[Category: Perbandt M]] | ||
| + | [[Category: Schneider T]] | ||
| + | [[Category: Schubert R]] | ||
Current revision
Low dose Thaumatin - 360-400 ms.
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