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Title
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Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium.
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Authors
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R.Reitzer,
M.Krasser,
G.Jogl,
W.Buckel,
H.Bothe,
C.Kratky.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
1039-1042.
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PubMed id
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Abstract
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Glutamate mutase [varepsilon2sigma2(B12)1] was reconstituted by incubating
purified components E (varepsilon2) and S (sigma2) 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 A and beta = 96.0 degrees for the
glutamate mutase reconstituted with aquocobalamin. They diffract to a resolution
of at least 2.7 A. 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 A. The crystals diffract to
about 3.2 A resolution. Native data sets were collected for both crystal forms.
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