Purification, crystallization and preliminary X-ray study of orotidine 5'-monophosphate decarboxylase

Acta Crystallogr D Biol Crystallogr. 2000 Jul;56(Pt 7):912-4. doi: 10.1107/s090744490000576x.

Abstract

Orotidine-5'-monophosphate decarboxylase (ODCase) from Methanobacterium thermoautotrophicum has been crystallized with and without the inhibitor 6-azaUMP by the vapour-diffusion method. In the absence of the inhibitor, the protein crystallizes in space group P4(1)2(1)2 (unit-cell parameters a = b = 56.9, c = 124.5 A) with one molecule per asymmetric unit; the crystals diffract to 1.8 A resolution. In the presence of the inhibitor, the protein crystals are monoclinic, space group P2(1) (unit-cell parameters a = 73.0, b = 98.6, c = 73.3 A, gamma = 104.0 degrees ), with four molecules in the asymmetric unit; the crystals diffract to 1.5 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Crystallography, X-Ray
  • DNA Primers
  • Methanobacterium / enzymology
  • Orotidine-5'-Phosphate Decarboxylase / chemistry*
  • Orotidine-5'-Phosphate Decarboxylase / isolation & purification*
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • DNA Primers
  • Recombinant Proteins
  • Orotidine-5'-Phosphate Decarboxylase