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Crystallization and preliminary X‐ray studies of ornithine decarboxylase from Trypanosoma brucei
Author(s) -
Grishin Nick V.,
Osterman Andrei L.,
Goldsmith Elizabeth J.,
Phillips Margaret A.
Publication year - 1996
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/(sici)1097-0134(199602)24:2<272::aid-prot17>3.0.co;2-k
Subject(s) - trypanosoma brucei , monoclinic crystal system , crystallography , crystallization , angstrom , chemistry , ornithine decarboxylase , crystal structure , enzyme , biochemistry , organic chemistry , gene
Trypanosoma brucei ornithine decarboxylase, expressed and purified from E. coli , has been crystallized by the vapor diffusion method using PEG 3350 as a precipitant. The crystals belong to the monoclinic space group P2 1 and have cell constants of a = 66.3 Å, b = 151.8 Å, c = 83.7 Å, and β = 101.2°. While larger crystals are twinned, smaller crystals (0.4 × 0.3 × 0.05 mm 3 ) are single.