Crystallization and preliminary X-ray diffraction analysis of cytochrome P450_sca-2 from Streptomyces carbophilus involved in production of pravastatin sodium, a tissue-selective inhibitor of HMG-CoA reductase

Cytochrome P450_sca-2 from Streptomyces carbophilus catalyzes the hydroxylation of ML-236B sodium salt to pravastatin sodium, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzymeA (HMG-CoA) reductase. HMG-CoA reductase is a key enzyme in cholesterol biosynthesis. Crystals of the protein were obtained by the vapour-diffusion method, using ammonium sulfate as a precipitant. The crystals belong to the trigonal space group P3₁21 (or its enantiomorph, P3₂21) with unit-cell dimensions a = 103.5, c = 79.8 Å. Assuming the presence of one molecule in the asymmetric unit, the calculated value of V_m is 2.68 Å³ Da^-1. A native data set was collected to a resolution of 2.2 Å.