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Crystallization and Preliminary X-Ray Diffraction Analysis of ARO9, an Aromatic Aminotransferase from Saccharomyces cerevisiae
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pp.450-453 (4) Authors: Hui Chen, Hua Huang, Xu Li, Shuilong Tong, Liwen Niu, Maikun Teng |
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| Abstract |
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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. |
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Keywords:
ARO9, aromatic aminotransferase, transamination, aminotransferase subgroup I, crystallization |
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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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