5map: Difference between revisions
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==X-ray generated oxyferrous complex of DtpA from Streptomyces lividans== | |||
<StructureSection load='5map' size='340' side='right'caption='[[5map]], [[Resolution|resolution]] 1.49Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5map]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans_TK24 Streptomyces lividans TK24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MAP 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]] 1.49Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=5map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5map OCA], [https://pdbe.org/5map PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5map RCSB], [https://www.ebi.ac.uk/pdbsum/5map PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5map ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into redox, ligand and spin states to complement the information gained from the electron-density maps. The correct assignment of crystal structures to the correct protein redox and ligand states is essential to avoid the misinterpretation of structural data. This is a particular concern for haem proteins, which can occupy a wide range of redox states and are exquisitely sensitive to becoming reduced by solvated electrons generated from interactions of X-rays with water molecules in the crystal. Here, single-crystal spectroscopic fingerprinting has been applied to investigate the laser photoreduction of ferric haem in cytochrome c'. Furthermore, in situ X-ray-driven generation of haem intermediates in crystals of the dye-decolourizing-type peroxidase A (DtpA) from Streptomyces lividans is described. | |||
Photoreduction and validation of haem-ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction.,Kekilli D, Moreno-Chicano T, Chaplin AK, Horrell S, Dworkowski FSN, Worrall JAR, Strange RW, Hough MA IUCrJ. 2017 Apr 10;4(Pt 3):263-270. doi: 10.1107/S2052252517002159. eCollection, 2017 May 1. PMID:28512573<ref>PMID:28512573</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5map" style="background-color:#fffaf0;"></div> | ||
[[Category: Chaplin | == References == | ||
[[Category: Hough | <references/> | ||
[[Category: Strange | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Streptomyces lividans TK24]] | |||
[[Category: Chaplin AK]] | |||
[[Category: Hough MA]] | |||
[[Category: Moreno Chicano T]] | |||
[[Category: Strange RW]] | |||
[[Category: Worrall JAR]] | |||
