Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus

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 (P2(1)2(1)2(1)) crystal forms have been grown with unit-cell dimensions a = 86.1, b = 146.7, c = 212.5 Angstrom and a = 84.8, b = 144.9, c = 203.0 Angstrom, Both crystals diffract to 2.3 Angstrom resolution using synchrotron radiation.