5lh5

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==High dose Thaumatin - 40-80 ms.==
==High dose Thaumatin - 40-80 ms.==
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<StructureSection load='5lh5' size='340' side='right' caption='[[5lh5]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
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<StructureSection load='5lh5' size='340' side='right'caption='[[5lh5]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5lh5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LH5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5lh5]] 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=5LH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LH5 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69&#8491;</td></tr>
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<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=5lh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lh5 OCA], [http://pdbe.org/5lh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lh5 RCSB], [http://www.ebi.ac.uk/pdbsum/5lh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lh5 ProSAT]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lh5 OCA], [https://pdbe.org/5lh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lh5 RCSB], [https://www.ebi.ac.uk/pdbsum/5lh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lh5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5lh5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Thaumatococcus daniellii]]
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[[Category: Betzel, C]]
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[[Category: Betzel C]]
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[[Category: Bourenkov, G]]
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[[Category: Bourenkov G]]
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[[Category: Giquel, Y]]
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[[Category: Giquel Y]]
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[[Category: Heymann, M]]
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[[Category: Heymann M]]
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[[Category: Kapis, S]]
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[[Category: Kapis S]]
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[[Category: Perbandt, M]]
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[[Category: Perbandt M]]
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[[Category: Schneider, T]]
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[[Category: Schneider T]]
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[[Category: Schubert, R]]
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[[Category: Schubert R]]
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[[Category: Multicrystal]]
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[[Category: Plant protein]]
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[[Category: Room-temperature]]
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[[Category: Thaumatin]]
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Current revision

High dose Thaumatin - 40-80 ms.

PDB ID 5lh5

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