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

机译:来自拟南芥的重组ACHT1:结晶和X射线晶体学分析

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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 Å 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 Å.
机译: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来执行其功能。 ACHT1(非典型的半胱氨酸/组氨酸富集的Trx1)是拟南芥叶绿体中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,通过蒸汽扩散法纯化和结晶。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该晶体属于C2221空间群,其晶胞参数a = 102.7,b = 100.6,c = 92.8。

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