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Protein and Peptide Letters

Volume 16 Issue 4
ISSN: 0929-8665

 

   All Titles

  Crystallization and Preliminary X-Ray Diffraction Analysis of ARO9, an Aromatic Aminotransferase from Saccharomyces cerevisiae
  pp.450-453 (4) Authors: Hui Chen, Hua Huang, Xu Li, Shuilong Tong, Liwen Niu, Maikun Teng
 
 
      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 P212121, with unit-cell parameters a = 75.6 Å, b = 117.5 Å, c = 134.9 Å. Diffraction data were collected to a resolution of 2.6 Å using a rotating-anode X-ray source. Analysis indicates the presence of two molecules in an asymmetric unit.

 
  Keywords: ARO9, aromatic aminotransferase, transamination, aminotransferase subgroup I, crystallization
  Affiliation: School of Life Science, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui, 230026, The People's Republic of China.
 
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