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The isolation, purification, and preliminary crystallographic characterization of udp‐galactose‐4‐epimerase from Escherichia coli
Author(s) -
Bauer Alan J.,
Rayment Ivan,
Frey Perry A.,
Holden Hazel M.
Publication year - 1991
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340090207
Subject(s) - orthorhombic crystal system , escherichia coli , uridine , polyethylene glycol , resolution (logic) , crystallography , enzyme , substrate (aquarium) , chemistry , stereochemistry , crystal structure , biochemistry , rna , biology , ecology , artificial intelligence , computer science , gene
Uridine diphosphogalactose‐4‐epimerase from E. coli has been crystallized in a form suitable for a high‐resolution X‐ray crystallographic structural analysis. The enzyme complexed with a substrate analogue, uridine diphosphobenzene (UDP‐benzene), crystallizes readily using polyethylene glycol 8000 as the precipitant. The crystals belong to the orthorhombic space group P 2 1 2 1 2 1 with unit cell dimensions, a = 76.3 Å, b = 83.1 Å, and c = 132.1 Å. Based on still setting photographs, the crystals diffract to a nominal resolution of 2.3 Å and are stable in the X‐ray beam. The enzyme used in these experiments was produced by a new expression system and a modified purification scheme.