Pan Weimin, Wang Junchao, Yang Ye, Liu Lin, Zhang Min
School of Life Sciences, Anhui University, 111 Jiulong Road, Hefei, Anhui 230026, People's Republic of China.
Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):382-385. doi: 10.1107/S2053230X17007725. Epub 2017 Jun 17.
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.
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。
