5fgx: Difference between revisions
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==Thaumatin solved by native sulphur SAD using synchrotron radiation== | |||
<StructureSection load='5fgx' size='340' side='right'caption='[[5fgx]], [[Resolution|resolution]] 2.13Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fgx]] 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=5FGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FGX 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]] 2.134Å</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=5fgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgx OCA], [https://pdbe.org/5fgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fgx RCSB], [https://www.ebi.ac.uk/pdbsum/5fgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fgx 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 == | |||
Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) offers unprecedented possibilities for macromolecular structure determination of systems that are prone to radiation damage. However, phasing XFEL data de novo is complicated by the inherent inaccuracy of SFX data, and only a few successful examples, mostly based on exceedingly strong anomalous or isomorphous difference signals, have been reported. Here, it is shown that SFX data from thaumatin microcrystals can be successfully phased using only the weak anomalous scattering from the endogenous S atoms. Moreover, a step-by-step investigation is presented of the particular problems of SAD phasing of SFX data, analysing data from a derivative with a strong anomalous signal as well as the weak signal from endogenous S atoms. | |||
Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data.,Nass K, Meinhart A, Barends TR, Foucar L, Gorel A, Aquila A, Botha S, Doak RB, Koglin J, Liang M, Shoeman RL, Williams G, Boutet S, Schlichting I IUCrJ. 2016 Mar 9;3(Pt 3):180-91. doi: 10.1107/S2052252516002980. eCollection, 2016 May 1. PMID:27158504<ref>PMID:27158504</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5fgx" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Botha | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thaumatococcus daniellii]] | ||
[[Category: | [[Category: Aquila A]] | ||
[[Category: | [[Category: Barends TRM]] | ||
[[Category: Meinhart | [[Category: Botha S]] | ||
[[Category: | [[Category: Boutet S]] | ||
[[Category: Schlichting | [[Category: Doak RB]] | ||
[[Category: | [[Category: Foucar L]] | ||
[[Category: | [[Category: Gorel A]] | ||
[[Category: Koglin J]] | |||
[[Category: Liang M]] | |||
[[Category: Meinhart A]] | |||
[[Category: Nass KJ]] | |||
[[Category: Schlichting I]] | |||
[[Category: Shoeman RL]] | |||
[[Category: Williams GJ]] | |||
Latest revision as of 09:50, 19 July 2023
Thaumatin solved by native sulphur SAD using synchrotron radiationThaumatin solved by native sulphur SAD using synchrotron radiation
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedSerial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) offers unprecedented possibilities for macromolecular structure determination of systems that are prone to radiation damage. However, phasing XFEL data de novo is complicated by the inherent inaccuracy of SFX data, and only a few successful examples, mostly based on exceedingly strong anomalous or isomorphous difference signals, have been reported. Here, it is shown that SFX data from thaumatin microcrystals can be successfully phased using only the weak anomalous scattering from the endogenous S atoms. Moreover, a step-by-step investigation is presented of the particular problems of SAD phasing of SFX data, analysing data from a derivative with a strong anomalous signal as well as the weak signal from endogenous S atoms. Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data.,Nass K, Meinhart A, Barends TR, Foucar L, Gorel A, Aquila A, Botha S, Doak RB, Koglin J, Liang M, Shoeman RL, Williams G, Boutet S, Schlichting I IUCrJ. 2016 Mar 9;3(Pt 3):180-91. doi: 10.1107/S2052252516002980. eCollection, 2016 May 1. PMID:27158504[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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