Reference: Chen H, et al. (2009) Crystallization and preliminary X-ray diffraction analysis of ARO9, an aromatic aminotransferase from Saccharomyces cerevisiae. Protein Pept Lett 16(4):450-3

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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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Chen H, Huang H, Li X, Tong S, Niu L, Teng M
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