Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium.
Acta Crystallogr D Biol Crystallogr
; 54(Pt 5): 1039-42, 1998 Sep 01.
Article
in En
| MEDLINE
| ID: mdl-9757132
ABSTRACT
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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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Conformation
/
Bacterial Proteins
/
Clostridium
/
Intramolecular Transferases
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
1998
Document type:
Article
Affiliation country:
Austria