Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium
Acta Crystallographica Section D
Volume 54, Issue 5, pages 1039–1042, September 1998
How to Cite
Reitzer, R., Krasser, M., Jogl, G., Buckel, W., Bothe, H. and Kratky, C. (1998), Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium. Acta Crystallographica Section D, 54: 1039–1042. doi: 10.1107/S0907444997020210
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Glutamate mutase [(B12)1] was reconstituted by incubating purified components E () and S () from Clostridium cochlearium, both produced in Escherichia coli, with either aquo- or cyanocobalamin. The inactive glutamate mutase obtained was crystallized with polyethyleneglycol 4000 as precipitant. Crystals are monoclinic with space group P21 and have cell dimensions a = 64.6, b = 113.2, c = 108.4 Å and β = 96.0° for the glutamate mutase reconstituted with aquocobalamin. They diffract to a resolution of at least 2.7 Å. Isolated component S was crystallized in the presence of an excess of cyanocobalamin, yielding red crystals of space group I422 with unit-cell dimensions of a = b = 69.9 and c = 107.1 Å. The crystals diffract to about 3.2 Å resolution. Native data sets were collected for both crystal forms.