Crystallization and preliminary X-ray diffraction analysis of omega-amino acid:pyruvate transaminase from Chromobacterium violaceum

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt 2):117-9. doi: 10.1107/S1744309107000863. Epub 2007 Jan 17.

Abstract

The enzyme omega-transaminase catalyses the conversion of chiral omega-amines to ketones. The recombinant enzyme from Chromobacterium violaceum has been purified to homogeneity. The enzyme was crystallized from PEG 4000 using the microbatch method. Data were collected to 1.7 A resolution from a crystal belonging to the triclinic space group P1, with unit-cell parameters a = 58.9, b = 61.9, c = 63.9 A, alpha = 71.9, beta = 87.0, gamma = 74.6 degrees . Data were also collected to 1.95 A from a second triclinic crystal form. The structure has been solved using the molecular-replacement method.

MeSH terms

  • Amino Acids / chemistry*
  • Amino Acids / metabolism
  • Chromobacterium / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Pyruvic Acid / chemistry*
  • Pyruvic Acid / metabolism
  • Transaminases / chemistry*
  • Transaminases / isolation & purification

Substances

  • Amino Acids
  • Pyruvic Acid
  • Transaminases

Associated data

  • PDB/1QJ3