Crystallization and X-ray diffraction analysis of peroxisomal Delta(3)-Delta(2)-enoyl-CoA isomerase from Saccharomyces cerevisiae

The purification, crystallization and X-ray diffraction analysis of Sacchar omyces cerevisiae Delta(3)-Delta(2)-enoyl-CoA isomerase is described. Delta (3)-Delta(2)-Enoyl-CoA isomerase is a member of the hydratase/isomerase pro tein family and is an auxiliary enzyme required for the beta-oxidation of u nsaturated fatty acids. It is a hexameric enzyme consisting of six identica l 32 kDa subunits of 280 residues each. In crystallization trials three cry stal forms were obtained, with tetragonal and hexagonal lattices. A 2.5 Ang strom data set was collected from the unliganded hexagonal crystals with an R-merge of 6.6%. The crystal, with unit-cell parameters a = 116.0, b = 116 .0, c = 122.9 Angstrom, is likely to have P6(3)22 symmetry.