CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF RECOMBINANT GLUTAMATE MUTASE AND OF THE ISOLATED COMPONENT-S FROM CLOSTRIDIUM-COCHLEARIUM

Glutamate mutase [epsilon(2)sigma(2)(B-12)(1)] was reconstituted by in cubating purified components E (epsilon(2)) and S (sigma(2)) from Clos tridium cochlearium, both produced in Escherichia coli, with either aq uo- or cyanocobalamin. The inactive glutamate mutase obtained was crys tallized with polyethyleneglycol 4000 as precipitant. Crystals are mon oclinic with space group P2(1) and have cell dimensions a = 64.6, b = 113.2, c = 108.4 Angstrom and beta = 96.0 degrees for the glutamate mu tase reconstituted with aquocobalamin. They diffract to a resolution o f at least 2.7 Angstrom. Isolated component S was crystallized in the presence of an excess of cyanocobalamin, yielding red crystals of spac e group I422 with unit-cell dimensions of a = b = 69.9 and c = 107.1 A ngstrom. The crystals diffract to about 3.2 Angstrom resolution. Nativ e data sets were collected for both crystal forms.