Crystallization and preliminary X-ray diffraction studies of a monooxygenase from Streptomyces coelicolor A3(2) involved in the biosynthesis of the polyketide actinorhodin

The aromatic monooxygenase ActVA-Orf6 from Streptomyces coelicolor A3(2) th at catalyses an unusual oxidation on the actinorhodin biosynthetic pathway has been crystallized. The crystals diffract to 1.73 Angstrom and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.95, b = 59.29, c = 71.67 Angstrom. Solvent-content (44%) and self-rotation function calcu lations predict the presence of two molecules in the asymmetric unit. Struc ture determination should provide further insight into the enzyme mechanism and aid in the design of biosynthetic pathways to produce new polyketide n atural products with novel functionality.