5wr8: Difference between revisions

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'''Unreleased structure'''


The entry 5wr8 is ON HOLD  until Paper Publication
==Thaumatin structure determined by SACLA at 1.55 Angstrom==
<StructureSection load='5wr8' size='340' side='right'caption='[[5wr8]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wr8]] 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=5WR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WR8 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]] 1.55&#8491;</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=5wr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wr8 OCA], [https://pdbe.org/5wr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wr8 RCSB], [https://www.ebi.ac.uk/pdbsum/5wr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wr8 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) allows structures of proteins to be determined at room temperature with minimal radiation damage. A highly viscous matrix acts as a crystal carrier for serial sample loading at a low flow rate that enables the determination of the structure, while requiring consumption of less than 1 mg of the sample. However, a reliable and versatile carrier matrix for a wide variety of protein samples is still elusive. Here we introduce a hydroxyethyl cellulose-matrix carrier, to determine the structure of three proteins. The de novo structure determination of proteinase K from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of the praseodymium atom was demonstrated using 3,000 diffraction images.


Authors:  
Hydroxyethyl cellulose matrix applied to serial crystallography.,Sugahara M, Nakane T, Masuda T, Suzuki M, Inoue S, Song C, Tanaka R, Nakatsu T, Mizohata E, Yumoto F, Tono K, Joti Y, Kameshima T, Hatsui T, Yabashi M, Nureki O, Numata K, Nango E, Iwata S Sci Rep. 2017 Apr 6;7(1):703. doi: 10.1038/s41598-017-00761-0. PMID:28386083<ref>PMID:28386083</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5wr8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Inoue S]]
[[Category: Masuda T]]
[[Category: Sugahara M]]
[[Category: Suzuki M]]

Latest revision as of 13:03, 6 September 2023

Thaumatin structure determined by SACLA at 1.55 AngstromThaumatin structure determined by SACLA at 1.55 Angstrom

Structural highlights

5wr8 is a 1 chain structure with sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.55Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.

Publication Abstract from PubMed

Serial femtosecond crystallography (SFX) allows structures of proteins to be determined at room temperature with minimal radiation damage. A highly viscous matrix acts as a crystal carrier for serial sample loading at a low flow rate that enables the determination of the structure, while requiring consumption of less than 1 mg of the sample. However, a reliable and versatile carrier matrix for a wide variety of protein samples is still elusive. Here we introduce a hydroxyethyl cellulose-matrix carrier, to determine the structure of three proteins. The de novo structure determination of proteinase K from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of the praseodymium atom was demonstrated using 3,000 diffraction images.

Hydroxyethyl cellulose matrix applied to serial crystallography.,Sugahara M, Nakane T, Masuda T, Suzuki M, Inoue S, Song C, Tanaka R, Nakatsu T, Mizohata E, Yumoto F, Tono K, Joti Y, Kameshima T, Hatsui T, Yabashi M, Nureki O, Numata K, Nango E, Iwata S Sci Rep. 2017 Apr 6;7(1):703. doi: 10.1038/s41598-017-00761-0. PMID:28386083[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Sugahara M, Nakane T, Masuda T, Suzuki M, Inoue S, Song C, Tanaka R, Nakatsu T, Mizohata E, Yumoto F, Tono K, Joti Y, Kameshima T, Hatsui T, Yabashi M, Nureki O, Numata K, Nango E, Iwata S. Hydroxyethyl cellulose matrix applied to serial crystallography. Sci Rep. 2017 Apr 6;7(1):703. doi: 10.1038/s41598-017-00761-0. PMID:28386083 doi:http://dx.doi.org/10.1038/s41598-017-00761-0

5wr8, resolution 1.55Å

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