Crystallization and preliminary X-ray diffraction analysis of ARO9, an aromatic aminotransferase from Saccharomyces cerevisiae.
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.
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Hui
H
Chen
Hua
H
Huang
Xu
X
Li
Shuilong
S
Tong
Liwen
L
Niu
Maikun
M
Teng
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D000637:Transaminases / Q000737:chemistry*
D029701:Saccharomyces cerevisiae Proteins; D000637:Transaminases; C541341:aromatic aminotransferase II, S cerevisiae