View source for 9hyz


==McCP in complex with photocaged nitric oxide, dark control, SSX==
<StructureSection load='9hyz' size='340' side='right'caption='[[9hyz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hyz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._Bath Methylococcus capsulatus str. Bath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HYZ 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9hyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hyz OCA], [https://pdbe.org/9hyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hyz RCSB], [https://www.ebi.ac.uk/pdbsum/9hyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hyz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G1UBD5_METCA G1UBD5_METCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Time-resolved X-ray crystallography is undergoing a renaissance due to the development of serial crystallography at synchrotron and XFEL beamlines. Crucial to such experiments are efficient and effective methods for uniformly initiating time-dependent processes within microcrystals, such as ligand binding, enzymatic reactions or signalling. A widely applicable approach is the use of photocaged substrates, where the photocage is soaked into the crystal in advance and then activated using a laser pulse to provide uniform initiation of the reaction throughout the crystal. This work characterizes photocage release of nitric oxide and binding of this ligand to two heme protein systems, cytochrome c'-beta and dye-decolourizing peroxidase B using a fixed target sample delivery system. Laser parameters for photoactivation are systematically explored, and time-resolved structures over timescales ranging from 100 micros to 1.4 s using synchrotron and XFEL beamlines are described. The effective use of this photocage for time-resolved crystallography is demonstrated and appropriate illumination conditions for such experiments are determined.

Time-resolved serial synchrotron and serial femtosecond crystallography of heme proteins using photocaged nitric oxide.,Smyth P, Jaho S, Williams LJ, Karras G, Fitzpatrick A, Thompson AJ, Battah S, Axford D, Horrell S, Lucic M, Ishihara K, Kataoka M, Matsuura H, Shimba K, Tono K, Tosha T, Sugimoto H, Owada S, Hough MA, Worrall JAR, Owen RL IUCrJ. 2025 Sep 1;12(Pt 5):582-594. doi: 10.1107/S2052252525006645. PMID:40843530<ref>PMID:40843530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9hyz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylococcus capsulatus str. Bath]]
[[Category: Hough MA]]
[[Category: Owen RL]]
[[Category: Smyth P]]
[[Category: Williams LJ]]
[[Category: Worrall JAR]]