Crystallization and Preliminary X-ray Data of Chloromuconate Cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4)

Abstract

The pJP4-encoded chloromuconate cycloisomerase, an enzyme of the 2,4-dichlorophenoxy-acetate degradation pathway, was purified from cell free extracts of Alcaligenes eutrophus JMP134 with a revised procedure. Tetragonal bipyramidal crystals were grown and characterized with respect to their X-ray diffraction properties. They were assigned to the space group I 4, with cell dimensions of a = b = 111·9 Å, c = 148·5 Å. The crystals scattered to approximately 3 Å resolution.