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

Vicki Bamford, Paul S. Dobbin, Sor Cheng Lee, Ann Reilly, Anne K. Powell, David J. Richardson, Andrew M. Hemmings

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4 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1222-1225
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Issue number6
Publication statusPublished - Jun 1999

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