title: Crystallization and preliminary X-ray studies of ornithine decarboxylase from Trypanosoma brucei.
abstract: 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 angstroms, b = 151.8 angstroms, c = 83.7 angstroms, and beta = 101.2 degrees. While larger crystals are twinned, smaller crystals (0.4 x 0.3 x 0.05 mm3) are single.
authors.affiliation: Department of Pharmacology, The University of Texas Southwestern Medical Center at Dallas, 75235-9041, USA.
authors.forename: N V
authors.initials: NV
authors.lastname: Grishin
authors.forename: A L
authors.initials: AL
authors.lastname: Osterman
authors.forename: E J
authors.initials: EJ
authors.lastname: Goldsmith
authors.forename: M A
authors.initials: MA
authors.lastname: Phillips
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D009955:Ornithine Decarboxylase / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D014346:Trypanosoma brucei brucei / Q000201:enzymology* / Q000235:genetics
chemical_list: D011994:Recombinant Proteins; D009955:Ornithine Decarboxylase