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Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):754-5.

Preliminary X-ray crystallographic study of DsrD protein from the sulfate-reducing bacterium Desulfovibrio vulgaris.

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Division of Chemistry, Graduate School of Science, Kyoto University, Sakyo, Japan.


DsrD (dissimilatory sulfite reductase D) protein encoded by the dsr operon of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough has been crystallized using the vapour-diffusion method with ammonium sulfate as a precipitating agent. The crystals diffract to 1.7 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 60.54 (6), b = 65. 20 (4), c = 46.41 (3) A. The crystal contains two DsrD molecules per asymmetric unit, giving a Matthews coefficient (V(M)) of 2.6 A(3) Da(-1). A gold-derivative (NaAuCl(4)) crystal has been successfully prepared.

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