首页> 外文期刊>Acta crystallographica. Section F, Structural biology communications >Recombinant ACHT1 from Arabidopsis thaliana: crystallization and X-ray crystallographic analysis
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Recombinant ACHT1 from Arabidopsis thaliana: crystallization and X-ray crystallographic analysis

机译:来自Arabidopsis的重组ACHT1:结晶和X射线晶体分析

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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.
机译:Thioredoxins(TRX)通过将光合光反应与一系列塑性功能联系起来,在叶绿体中起着重要作用。 它们通过调节氧化和减少二硫键来执行它们的功能。 ACHT1(非典型半胱氨酸/组氨酸的TRX1)是在拟南芥叶绿体中发现的囊体相关的嗜毒素蛋白。 重组ACHT1蛋白在大肠杆菌中过表达,通过蒸汽扩散法纯化并结晶。 收集晶体衍射至1.7埃千埃分辨率,并收集完整的X射线数据集。 初步晶体分析表明,晶体属于空间组C2221,具有单位电池参数A = 102.7,B = 100.6,C = 92.8埃。

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