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来自拟南芥的重组ACHT1:结晶及X射线晶体学分析

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

作者信息

Pan Weimin, Wang Junchao, Yang Ye, Liu Lin, Zhang Min

机构信息

School of Life Sciences, Anhui University, 111 Jiulong Road, Hefei, Anhui 230026, People's Republic of China.

出版信息

Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):382-385. doi: 10.1107/S2053230X17007725. Epub 2017 Jun 17.

Abstract

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 Å resolution and a complete X-ray data set was collected. Preliminary crystallographic analysis suggested that the crystals belonged to space group C222, with unit-cell parameters a = 102.7, b = 100.6, c = 92.8 Å.

摘要

硫氧还蛋白(Trxs)通过将光合光反应与一系列质体功能联系起来,在叶绿体中发挥重要作用。它们通过调节二硫键的氧化和还原发挥功能。ACHT1(富含非典型半胱氨酸/组氨酸的Trx1)是一种在拟南芥叶绿体中发现的与类囊体相关的硫氧还蛋白型蛋白。重组ACHT1蛋白在大肠杆菌中过表达,通过气相扩散法纯化并结晶。晶体衍射至1.7 Å分辨率,并收集了完整的X射线数据集。初步晶体学分析表明,晶体属于空间群C222,晶胞参数a = 102.7,b = 100.6,c = 92.8 Å。

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