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

被引：4
|
作者：
Chen, Hui [1 ,2 ,3 ]
Huang, Hua [1 ,2 ,3 ]
Li, Xu [1 ,2 ,3 ]
Tong, Shuilong [1 ,2 ,3 ]
Niu, Liwen [1 ,2 ,3 ]
Teng, Maikun [1 ,2 ,3 ]
机构：
[1] Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui, Peoples R China
[2] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China
[3] Chinese Acad Sci, Key Lab Struct Biol, Hefei 230026, Anhui, Peoples R China
来源：
PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 04期
关键词：
ARO9; aromatic aminotransferase; transamination; aminotransferase subgroup I; crystallization; CRYSTAL-STRUCTURE; PROTEINS; DNA;
D O I：
10.2174/092986609787848036
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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 angstrom, b = 117.5 angstrom, c = 134.9 angstrom. Diffraction data were collected to a resolution of 2.6 angstrom using a rotating-anode X-ray source. Analysis indicates the presence of two molecules in an asymmetric unit.
引用
收藏
页码：450 / 453
页数：4
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