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

页码：450 / 453

页数：4

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