Recombinant ACHT1 from Arabidopsis thaliana: crystallization and X-ray crystallographic analysis

被引:1
|
作者
Pan, Weimin [1 ]
Wang, Junchao [1 ]
Yang, Ye [1 ]
Liu, Lin [1 ]
Zhang, Min [1 ]
机构
[1] Anhui Univ, Sch Life Sci, 111 Jiulong Rd, Hefei 230026, Anhui, Peoples R China
关键词
thioredoxins; photosynthetic light reactions; Arabidopsis thaliana; disulfide bonds; chloroplasts; ACHT1; 3-DIMENSIONAL STRUCTURE; THIOREDOXINS; GLUTAREDOXINS; RESOLUTION; PLANTS;
D O I
10.1107/S2053230X17007725
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Thioredoxins (Trxs) play important roles in chloroplasts by linking photosynthetic light reactions to a series of plastid functions. They execute their function by regulating the oxidation and reduction of disulfide bonds. ACHT1 (atypical cysteine/histidine-rich Trx1) is a thylakoid-associated thioredoxin-type protein found in the Arabidopsis thaliana chloroplast. Recombinant ACHT1 protein was overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method. The crystal diffracted to 1.7 angstrom resolution and a complete X-ray data set was collected. Preliminary crystallographic analysis suggested that the crystals belonged to space group C2221, with unit-cell parameters a = 102.7, b = 100.6, c = 92.8 angstrom.
引用
收藏
页码:382 / 385
页数:4
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