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

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 Å resolution and belong to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 60.54 (6), b = 65.20 (4), c = 46.41 (3) Å. The crystal contains two DsrD molecules per asymmetric unit, giving a Matthews coefficient (V_M) of 2.6 Å³ Da^-1. A gold-derivative (NaAuCl₄) crystal has been successfully prepared.