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Bamford, Vicki, Dobbin, Paul S., Lee, Sor Cheng, Reilly, Ann, Powell, Anne K., Richardson, David J. 
ORCID: https://orcid.org/0000-0002-6847-1832 and Hemmings, Andrew M. ORCID: https://orcid.org/0000-0003-3053-3134
(1999)
Crystallization and preliminary X-ray crystallographic analysis of a periplasmic tetrahaem flavocytochrome c3 from Shewanella frigidimarina NCIMB400 which has fumarate reductase activity.
Acta Crystallographica Section D: Biological Crystallography, 55 (6).
pp. 1222-1225.
ISSN 0907-4449
Abstract
The fumarate reductase of Escherichia coli and other bacteria is a membrane-bound enzyme consisting of four subunits. A soluble periplasmic 64 kDa tetrahaem flavocytochrome c3 from Shewanella frigidimarina NCIMB400 which possesses a catalytic fumarate reductase activity has been crystallized. The crystals belong to space group P212121 with unit-cell parameters a = 72.4, b = 110.1, c = 230.2 Å. Assuming a molecular dimer in the asymmetric unit, the crystals contain 65% solvent and, when cryocooled to 100 K, the crystals diffract to at least 3.0 Å resolution. The crystals, however, display an inherent lack of isomorphism and the plausibility of a MAD phasing experiment has therefore been investigated by measuring the iron K absorption edge from a single crystal.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | structural biology ,/dk/atira/pure/subjectarea/asjc/1300/1315 |
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 15 Jul 2022 11:30 |
| Last Modified: | 15 May 2023 00:54 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/86181 |
| DOI: | 10.1107/S0907444999004114 |
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