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==Copper nitrite reductase from Achromobacter cycloclastes: non-polymorph separated dataset 1== | ==Copper nitrite reductase from Achromobacter cycloclastes: non-polymorph separated dataset 1== | ||
<StructureSection load='6gby' size='340' side='right' caption='[[6gby]], [[Resolution|resolution]] 1.48Å' scene=''> | <StructureSection load='6gby' size='340' side='right'caption='[[6gby]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6gby]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GBY FirstGlance]. <br> | <table><tr><td colspan='2'>[[6gby]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_cycloclastes"_(gray_and_thornton)_bergey_et_al. "achromobacter cycloclastes" (gray and thornton) bergey et al.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GBY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nirK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223 "Achromobacter cycloclastes" (Gray and Thornton) Bergey et al.])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gby OCA], [http://pdbe.org/6gby PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gby RCSB], [http://www.ebi.ac.uk/pdbsum/6gby PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gby ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gby OCA], [http://pdbe.org/6gby PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gby RCSB], [http://www.ebi.ac.uk/pdbsum/6gby PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gby ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ability to determine high-quality, artefact-free structures is a challenge in micro-crystallography, and the rapid onset of radiation damage and requirement for a high-brilliance X-ray beam mean that a multi-crystal approach is essential. However, the combination of crystal-to-crystal variation and X-ray-induced changes can make the formation of a final complete data set challenging; this is particularly true in the case of metalloproteins, where X-ray-induced changes occur rapidly and at the active site. An approach is described that allows the resolution, separation and structure determination of crystal polymorphs, and the tracking of radiation damage in microcrystals. Within the microcrystal population of copper nitrite reductase, two polymorphs with different unit-cell sizes were successfully separated to determine two independent structures, and an X-ray-driven change between these polymorphs was followed. This was achieved through the determination of multiple serial structures from microcrystals using a high-throughput high-speed fixed-target approach coupled with robust data processing. | |||
Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography.,Ebrahim A, Appleby MV, Axford D, Beale J, Moreno-Chicano T, Sherrell DA, Strange RW, Hough MA, Owen RL Acta Crystallogr D Struct Biol. 2019 Feb 1;75(Pt 2):151-159. doi:, 10.1107/S2059798318010240. Epub 2018 Nov 9. PMID:30821704<ref>PMID:30821704</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6gby" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Appleby, M V]] | [[Category: Appleby, M V]] | ||
[[Category: Axford, D]] | [[Category: Axford, D]] | ||
Latest revision as of 15:39, 13 March 2019
Copper nitrite reductase from Achromobacter cycloclastes: non-polymorph separated dataset 1Copper nitrite reductase from Achromobacter cycloclastes: non-polymorph separated dataset 1
Structural highlights
Publication Abstract from PubMedThe ability to determine high-quality, artefact-free structures is a challenge in micro-crystallography, and the rapid onset of radiation damage and requirement for a high-brilliance X-ray beam mean that a multi-crystal approach is essential. However, the combination of crystal-to-crystal variation and X-ray-induced changes can make the formation of a final complete data set challenging; this is particularly true in the case of metalloproteins, where X-ray-induced changes occur rapidly and at the active site. An approach is described that allows the resolution, separation and structure determination of crystal polymorphs, and the tracking of radiation damage in microcrystals. Within the microcrystal population of copper nitrite reductase, two polymorphs with different unit-cell sizes were successfully separated to determine two independent structures, and an X-ray-driven change between these polymorphs was followed. This was achieved through the determination of multiple serial structures from microcrystals using a high-throughput high-speed fixed-target approach coupled with robust data processing. Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography.,Ebrahim A, Appleby MV, Axford D, Beale J, Moreno-Chicano T, Sherrell DA, Strange RW, Hough MA, Owen RL Acta Crystallogr D Struct Biol. 2019 Feb 1;75(Pt 2):151-159. doi:, 10.1107/S2059798318010240. Epub 2018 Nov 9. PMID:30821704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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