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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
Hui Chen 1 , Hua Huang , Xu Li , Shuilong Tong , Liwen Niu , Maikun Teng
Hui Chen 1 , Hua Huang , Xu Li , Shuilong Tong , Liwen Niu , Maikun Teng
+ et al

[No authors listed]

Author information
  • 1 Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.

摘要


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.