Crystallization and X-ray diffraction analysis of peroxisomal D-D-enoyl-CoA isomerase from Saccharomyces cerevisiae

# 2000 International Union of Crystallography Printed in Denmark ± all rights reserved The puri®cation, crystallization and X-ray diffraction analysis of Saccharomyces cerevisiae -enoyl-CoA isomerase is described. -Enoyl-CoA isomerase is a member of the hydratase/isomerase protein family and is an auxiliary enzyme required for the -oxidation of unsaturated fatty acids. It is a hexameric enzyme consisting of six identical 32 kDa subunits of 280 residues each. In crystallization trials three crystal forms were obtained, with tetragonal and hexagonal lattices. A 2.5 AÊ data set was collected from the unliganded hexagonal crystals with an Rmerge of 6.6%. The crystal, with unit-cell parameters a = 116.0, b = 116.0, c = 122.9 AÊ , is likely to have P6322 symmetry. Received 19 January 2000 Accepted 27 April 2000