View source for 8wxn


==Crystal structure of substrate-binding protein from Rhodothermus marinus (Dose II)==
<StructureSection load='8wxn' size='340' side='right'caption='[[8wxn]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8wxn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus_DSM_4252 Rhodothermus marinus DSM 4252]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WXN 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]] 1.58&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=8wxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wxn OCA], [https://pdbe.org/8wxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wxn RCSB], [https://www.ebi.ac.uk/pdbsum/8wxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wxn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D0MDR1_RHOM4 D0MDR1_RHOM4] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Radiation damage is an inherent issue in X-ray crystallography. It not only damages macromolecular crystals, which lowers the quality of the diffraction intensity, but results in inaccurate structural information. Among the various types of radiation damage, little is known regarding the damage to selenomethionine, an amino acid contained in some proteins. Recently, radiation damage to the selenomethionine-substituted single-domain substrate-binding domain from Rhodothermus marinus (SeMet-RmSBP) was investigated. Global and specific radiation damage from four datasets collected by repeatedly exposing a single RmSBP-SeMet crystal to X-rays were analyzed. The results indicated that the B-factor value of the selenium atom in selenomethionine was significantly increased compared with other atoms. To date, no images of radiation damage have been reported for selenomethionine-substituted proteins. Therefore, these data may be used to study radiation damage in macromolecular crystallography. This study provides insight into radiation damage associated with selenomethionine.

Data of radiation damage on selenomethionine-substituted single-domain substrate-binding protein.,Nam KH Data Brief. 2024 Jan 30;53:110114. doi: 10.1016/j.dib.2024.110114. eCollection , 2024 Apr. PMID:38348329<ref>PMID:38348329</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8wxn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodothermus marinus DSM 4252]]
[[Category: Nam KH]]