首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus
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Crystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus

机译:激烈热球菌和嗜热栖热菌推定的tRNA修饰酶的结晶和初步X射线晶体学分析

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摘要

Methyltransferases form a major class of tRNA-modifying enzymes that are needed for the proper functioning of tRNA. Here, the expression, purification and crystallization of two related putative tRNA methyltransferases from two kingdoms of life are reported. The protein encoded by the gene pf1002 from the archaeon Pyrococcus furiosus was crystallized in the monoclinic space group P21. A complete data set was collected to 2.2 Å resolution. The protein encoded by the gene ttc1157 from the eubacterium Thermus thermophilus was crystallized in the trigonal space group P3221. A complete data set was collected to 2.05 Å resolution.
机译:甲基转移酶是tRNA正常运行所必需的一类主要的tRNA修饰酶。在此,报道了来自两个生命王国的两个相关推定的tRNA甲基转移酶的表达,纯化和结晶。由古细菌热球菌(Pyrococcus furiosus)的pf1002基因编码的蛋白质在单斜空间群P21中结晶。收集了一个完整的数据集,分辨率达到了2.2Å。真热嗜热杆菌的ttc1157基因编码的蛋白质在三角空间群P3221中结晶。收集了一个完整的数据集,分辨率为2.05Å。

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