Crystallization and preliminary X-ray diffraction analysis of ARO9, an aromatic aminotransferase from Saccharomyces cerevisiae

Protein Pept Lett. 2009;16(4):450-3. doi: 10.2174/092986609787848036.

Abstract

Saccharomyces cerevisae ARO9 protein, an aromatic aminotransferase II, catalyzes the transamination step of the catabolism of aromatic amino acids, mainly tryptophan. ARO9 also belongs to a novel subfamily of enzymes within the aminotransferase subgroup I. Crystals of ARO9 protein have been grown using the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 75.6 A, b = 117.5 A, c = 134.9 A. Diffraction data were collected to a resolution of 2.6 A using a rotating-anode X-ray source. Analysis indicates the presence of two molecules in an asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transaminases / chemistry*

Substances

  • Saccharomyces cerevisiae Proteins
  • Transaminases
  • aromatic aminotransferase II, S cerevisiae