RESUMO
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 277â K using the sitting-drop vapour-diffusion method with PEG 3350 and potassium thiocyanate as precipitants. A data set was collected to 3.7â Å resolution from a single crystal at 100â 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 = 435.32â 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)ß(2)γ(2) units per asymmetric unit, with a Matthews coefficient (V(M)) of 2.35â Å(3)â Da(-1); the solvent content was estimated to be 47.7%.
Assuntos
Desulfovibrio vulgaris/enzimologia , Sulfito de Hidrogênio Redutase/química , Cristalização , Cristalografia por Raios X , Sulfito de Hidrogênio Redutase/isolamento & purificação , Modelos Moleculares , Estrutura Terciária de ProteínaRESUMO
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%.
