Purification, crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Desulfovibrio vulgaris Miyazaki F.
Sulfur in its various oxidation states is used for energy conservation in many microorganisms. Adenylylsulfate reductase is a key enzyme in the sulfur-reduction pathway of sulfate-reducing bacteria. The adenylylsulfate reductase from Desulfovibrio vulgaris Miyazaki F has been purified and crystallized at 277 K using the vapour-diffusion method with ammonium sulfate as the precipitating agent. A data set was collected to 1.7 A resolution from a single crystal at 100 K using synchrotron radiation. The crystal belonged to space group P3(1), with unit-cell parameters a = b = 125.93, c = 164.24 A. The crystal contained two molecules per asymmetric unit, with a Matthews coefficient (V(M)) of 4.02 A(3) Da(-1); the solvent content was estimated to be 69.4%.
Ogata
Hideaki
H
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
Goenka Agrawal
Aruna
A
Kaur
Amrit Pal
AP
Goddard
Richard
R
Gärtner
Wolfgang
W
Lubitz
Wolfgang
W
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003460:Crystallization / Q000379:methods; D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D008969:Molecular Sequence Data; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors; C019618:adenylylsulfate reductase