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 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.
Mizuno
N
N
Division of Chemistry, Graduate School of Science, Kyoto University, Sakyo, Japan.
Hittel
D S
DS
Miki
K
K
Voordouw
G
G
Higuchi
Y
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D050885:Hydrogensulfite Reductase; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry* / Q000302:isolation & purification
D050862:Oxidoreductases Acting on Sulfur Group Donors; D050885:Hydrogensulfite Reductase