1. Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus
- Author
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Juan C. Fontecilla-Camps, Claude E. Hatchikian, M.H. Charon, Eric Chabrière, and Laetitia Pieulle
- Subjects
chemistry.chemical_classification ,Pyruvate decarboxylation ,biology ,Pyruvate Synthase ,Ketone Oxidoreductases ,General Medicine ,Polyethylene glycol ,biology.organism_classification ,Crystallography, X-Ray ,law.invention ,Crystal ,Crystallography ,chemistry.chemical_compound ,Enzyme ,chemistry ,Structural Biology ,Oxidoreductase ,law ,Orthorhombic crystal system ,Desulfovibrio ,Crystallization ,Energy Metabolism ,Bacteria - Abstract
For the first time, crystals of a pyruvate-ferredoxin oxidoreductase (PFOR) suitable for X-ray analysis have been obtained. This enzyme catalyzes, in anaerobic organisms, the crucial energy-yielding reaction of pyruvate decarboxylation to acetylCoA. Polyethylene glycol and divalent metal cations have been used to crystallize the PFOR from the sulfate-reducing bacterium Desulfovibrio africanus. Two different orthorhombic (P212121 ) crystal forms have been grown with unit-cell dimensions a = 86.1, b = 146.7, c = 212.5 A and a = 84.8, b = 144.9, c = 203.0 A. Both crystals diffract to 2.3 A resolution using synchrotron radiation.
- Published
- 1998