Crystallization and preliminary X-ray crystallographic analysis of a periplasmic tetrahaem flavocytochrome c3 from Shewanella frigidimarina NCIMB400 which has fumarate reductase activity

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

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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
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 15 Jul 2022 11:30
Last Modified: 13 Aug 2022 02:20
URI: https://ueaeprints.uea.ac.uk/id/eprint/86181
DOI: 10.1107/S0907444999004114

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