Crystallization and preliminary X-ray diffraction studies of maleylacetate reductase from Rhizobium sp strain MTP-10005

Maleylacetate reductase (EC 1.3.1.32), which catalyzes the reduction of maleylacetate to 3-oxoadipate, plays an important role in the aerobic microbial catabolism of resorcinol. The enzyme has been crystallized at 293 K by the sitting-drop vapour-diffusion method supplemented with a microseeding technique, using ammonium sulfate as the precipitating agent. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 56.85, b = 121.13, c = 94.09 angstrom, beta = 101.48 degrees, and contained one dimeric molecule in the asymmetric unit. It diffracted to 1.79 angstrom resolution.