GPX3 from Arabidopsis thaliana: cloning, expression, purification, crystallization and preliminary X-ray analysis

被引:4
作者
Li, Kun [1 ]
Yang, Qingzhan [2 ]
Wang, Wei [1 ]
Zhao, Xiaoliang [1 ]
Lou, Zhiyong [2 ]
机构
[1] Henan Univ, Dept Biol, Henan Key Lab Plant Stress Biol, Kaifeng 475001, Peoples R China
[2] Tsinghua Univ, Sch Med, Struct Biol Lab, Beijing 100084, Peoples R China
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
关键词
HYDROPEROXIDE GLUTATHIONE-PEROXIDASE; THIOREDOXIN PEROXIDASE; OXIDATIVE STRESS; ACTIVE OXYGEN; PROTEIN; CITRUS; CDNA;
D O I
10.1107/S1744309113025566
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The Arabidopsis thaliana glutathione peroxidase 3 (GPX3) gene encodes a glutathione peroxidase with roles in H2O2 homeostasis and signalling. The GPX3 gene sequence was cloned into pGEX-6P1 and overexpressed in Escherichia coli. The GPX3 protein was purified to homogeneity in two chromatographic steps. Various lengths of the GPX3 sequence were used to obtain proteins that yielded crystals using vapour-diffusion techniques, but only GPX3 Delta N36 (lacking 36 amino acids from the N-terminus) showed a good diffraction pattern. Its crystals diffracted to 2.8 angstrom resolution and belonged to space group P6(5), with unit-cell parameters a = b = 98.241, c = 42.057 angstrom.
引用
收藏
页码:1224 / 1226
页数:3
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