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Expression purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis

机译:结核分枝杆菌精氨酸阻遏蛋白C末端结构域的表达纯化和初步X射线分析

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摘要

The gene product of an open reading frame Rv1657 from Mycobacterium tuberculosis is a putative arginine repressor protein (ArgR), a transcriptional factor that regulates the expression of arginine-biosynthetic enzymes. Rv1657 was expressed and purified and a C-terminal domain was crystallized using the hanging-drop vapour-diffusion method. Diffraction data were collected and processed to a resolution of 2.15 Å. The crystals belong to space group P1 and the Matthews coefficient suggests that the crystals contain six C-­terminal domain molecules per unit cell. Previous structural and biochemical studies on the arginine repressor proteins from other organisms have likewise shown the presence of six molecules per unit cell.
机译:来自结核分枝杆菌的开放阅读框Rv1657的基因产物是推定的精氨酸阻遏蛋白(ArgR),这是一种调节精氨酸生物合成酶表达的转录因子。表达和纯化Rv1657,并使用悬滴蒸气扩散法结晶C末端结构域。收集衍射数据并将其处理为2.15Å的分辨率。晶体属于空间群P1,马修斯系数表明该晶体每单位细胞包含六个C-­端域分子。先前对来自其他生物的精氨酸阻遏蛋白的结构和生化研究同样表明,每单位细胞中存在六个分子。

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