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6GBY

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

Summary for 6GBY
Entry DOI10.2210/pdb6gby/pdb
DescriptorCopper-containing nitrite reductase, COPPER (II) ION, NITRITE ION, ... (4 entities in total)
Functional Keywordscopper, denitrification, serial synchrotron crystallography, polymorphs, nitrite reductase, oxidoreductase
Biological sourceAchromobacter cycloclastes
Total number of polymer chains1
Total formula weight40992.27
Authors
Ebrahim, A.,Appleby, M.V.,Axford, D.,Beale, J.,Moreno-Chicano, T.,Sherrell, D.A.,Strange, R.W.,Owen, R.L.,Hough, M.A. (deposition date: 2018-04-16, release date: 2019-01-30, Last modification date: 2024-01-17)
Primary citationEbrahim, A.,Appleby, M.V.,Axford, D.,Beale, J.,Moreno-Chicano, T.,Sherrell, D.A.,Strange, R.W.,Hough, M.A.,Owen, R.L.
Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography.
Acta Crystallogr D Struct Biol, 75:151-159, 2019
Cited by
PubMed Abstract: 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.
PubMed: 30821704
DOI: 10.1107/S2059798318010240
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.48 Å)
Structure validation

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