Purification, crystallization and preliminary X-ray analysis of the dissimilatory sulfite reductase from Desulfovibrio vulgaris Miyazaki F.
Dissimilatory sulfite reductase (Dsr) plays an important role in sulfate respiration in many sulfate-reducing bacteria. Dsr from Desulfovibrio vulgaris Miyazaki F has been purified and crystallized at 277 K using the sitting-drop vapour-diffusion method with PEG 3350 and potassium thiocyanate as precipitants. A data set was collected to 3.7 Å resolution from a single crystal at 100 K using synchrotron radiation. The Dsr crystal belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 163.26, c = 435.32 Å. The crystal structure of Dsr was determined by the molecular-replacement method based on the three-dimensional structure of Dsr from D. vulgaris Hildenborough. The crystal contained three α(2)β(2)γ(2) units per asymmetric unit, with a Matthews coefficient (V(M)) of 2.35 Å(3) Da(-1); the solvent content was estimated to be 47.7%.
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
Hideaki
H
Ogata
Yasuhito
Y
Shomura
Aruna
A
Goenka Agrawal
Amrit Pal
AP
Kaur
Wolfgang
W
Gärtner
Yoshiki
Y
Higuchi
Wolfgang
W
Lubitz
D003460:Crystallization; D018360:Crystallography, X-Ray; D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D050885:Hydrogensulfite Reductase / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D017434:Protein Structure, Tertiary
D050885:Hydrogensulfite Reductase