9t6p: Difference between revisions
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==Higher-dose (283.1 kGy) structure of copper-containing nitrite reductase from Achromobacter cycloclastes at room temperature== | |||
<StructureSection load='9t6p' size='340' side='right'caption='[[9t6p]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9t6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9T6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9T6P 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]] 2.008Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9t6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9t6p OCA], [https://pdbe.org/9t6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9t6p RCSB], [https://www.ebi.ac.uk/pdbsum/9t6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9t6p ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NIR_ACHCY NIR_ACHCY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Specific radiation damage (SRD) to proteins is a pertinent issue discovered during the development of cryo-crystallography at synchrotrons, often affecting the macromolecular active site and thus complicating the understanding of mechanistic insights from structural analysis. For proteins with a spectroscopic signature in the visible light spectrum, in crystallo UV-Vis absorption spectroscopy has regularly been used to estimate the dose scale of specific damage build-up and to develop diffraction data-collection strategies to mitigate its effects. Using a coupled spectroscopic and crystallographic approach, here we show that for two metal-containing proteins the structural response to X-ray-induced reduction of metals in their active site is markedly different at room temperature than at cryogenic temperature. This suggests that the use of controlled specific radiation damage to mimic and study a physiological redox transition in a metal-containing protein by X-ray crystallography should preferably be performed at room temperature rather than at cryogenic temperature. | |||
Coupled on-line in crystallo UV-Vis absorption spectroscopy and X-ray crystallography to compare specific radiation damage in metal-containing proteins at room versus cryogenic temperature.,Caramello N, Rose SL, Mathieu E, Petit L, Tews I, Engilberge S, Royant A Acta Crystallogr D Struct Biol. 2026 Mar 1;82(Pt 3):187-198. doi: , 10.1107/S2059798326000690. Epub 2026 Feb 5. PMID:41641581<ref>PMID:41641581</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9t6p" style="background-color:#fffaf0;"></div> | ||
[[Category: Engilberge | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Achromobacter cycloclastes]] | |||
[[Category: Large Structures]] | |||
[[Category: Caramello N]] | |||
[[Category: Engilberge S]] | |||
[[Category: Rose SL]] | |||
[[Category: Royant A]] | |||
