Crystallization and preliminary X-ray studies of ornithine decarboxylase from Trypanosoma brucei

Proteins. 1996 Feb;24(2):272-3. doi: 10.1002/(SICI)1097-0134(199602)24:2<272::AID-PROT17>3.0.CO;2-K.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Ornithine Decarboxylase / chemistry*
  • Ornithine Decarboxylase / genetics
  • Recombinant Proteins / chemistry
  • Trypanosoma brucei brucei / enzymology*
  • Trypanosoma brucei brucei / genetics

Substances

  • Recombinant Proteins
  • Ornithine Decarboxylase