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

N Mizuno; D S Hittel; K Miki; G Voordouw; Y Higuchi

doi:10.1107/s0907444900004327

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

Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):754-5. doi: 10.1107/s0907444900004327.

Authors

N Mizuno¹, D S Hittel, K Miki, G Voordouw, Y Higuchi

Affiliation

¹ Division of Chemistry, Graduate School of Science, Kyoto University, Sakyo, Japan.

PMID: 10818354
DOI: 10.1107/s0907444900004327

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray
Desulfovibrio vulgaris / enzymology*
Hydrogensulfite Reductase
Oxidoreductases Acting on Sulfur Group Donors / chemistry*
Oxidoreductases Acting on Sulfur Group Donors / isolation & purification

Substances

Oxidoreductases Acting on Sulfur Group Donors
Hydrogensulfite Reductase