Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina.
The fumarate reductase (flavocytochrome c(3)) from Shewanella frigidimarina (formerly S. putrefaciens) NCIMB400 has been crystallized in the space group P2(1), with cell dimensions of a = 45.447 A, b = 92.107 A, c = 78.311 A, and beta = 91.038 degrees and one molecule per asymmetric unit. A native data set has been collected to 1.8 A. The gene encoding Fcc(3) from the S. frigidimarina type strain ACAM591 has been cloned and sequenced and the protein crystallized in space group P2(1) with cell dimensions of a = 45.359 A, b = 88.051 A, c = 77.473 A, and beta = 104.499 degrees. Anomalous data have also been collected from the NCIMB400 crystal allowing the heme iron positions to be identified.
Pealing
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Department of Chemistry, University of Edinburgh, Edinburgh, Scotland, United Kingdom.
Lysek
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Taylor
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Alexeev
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Reid
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Chapman
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Walkinshaw
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D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry*; D005290:Ferric Compounds; D006092:Gram-Negative Facultatively Anaerobic Rods / Q000737:chemistry / Q000201:enzymology; D006418:Heme; D011487:Protein Conformation; D017422:Sequence Analysis, DNA; D013385:Succinate Dehydrogenase / Q000737:chemistry*
D003574:Cytochrome c Group; D005290:Ferric Compounds; D006418:Heme; C112400:flavocytochrome c3; D013385:Succinate Dehydrogenase