6gby

Copper nitrite reductase from Achromobacter cycloclastes: non-polymorph separated dataset 1

spinqualitylabelsall models 6gby, resolution 1.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gby is a 1 chain structure with sequence from "achromobacter_cycloclastes"_(gray_and_thornton)_bergey_et_al. "achromobacter cycloclastes" (gray and thornton) bergey et al.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, NO2 Gene: nirK ("Achromobacter cycloclastes" (Gray and Thornton) Bergey et al.) Activity: Nitrite reductase (NO-forming), with EC number 1.7.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA