Crystallization and Preliminary X-Ray Diffraction Analysis of ARO9, an Aromatic Aminotransferase from Saccharomyces cerevisiae

Title: Crystallization and Preliminary X-Ray Diffraction Analysis of ARO9, an Aromatic Aminotransferase from Saccharomyces cerevisiae

Volume: 16 Issue: 4

Author(s): Hui Chen, Hua Huang, Xu Li, Shuilong Tong, Liwen Niu and Maikun Teng

Affiliation:

Keywords: ARO9, aromatic aminotransferase, transamination, aminotransferase subgroup I, crystallization

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.

Cite this article as:

Chen Hui, Huang Hua, Li Xu, Tong Shuilong, Niu Liwen and Teng Maikun, Crystallization and Preliminary X-Ray Diffraction Analysis of ARO9, an Aromatic Aminotransferase from Saccharomyces cerevisiae, Protein & Peptide Letters 2009; 16 (4) . https://dx.doi.org/10.2174/092986609787848036