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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization of the xeroderma pigmentosum group F endonuclease from Aeropyrum pernix
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Crystallization of the xeroderma pigmentosum group F endonuclease from Aeropyrum pernix

机译:着色性干皮病组的结晶F核酸内切酶从Aeropyrum pernix

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摘要

The xeroderma pigmentosa group F protein (XPF) is a founding member of a family of 3'-flap endonucleases that play an essential role in nucleotide-excision repair, DNA replication and recombination. The XPF gene has been cloned from Aeropyrum pernix, encoding a 254-residue protein (apXPF). Recombinant protein was produced in Escherichia coli and purified by three chromatographic steps. Three different crystal forms of apXPF were grown in trigonal, monoclinic and triclinic systems. The trigonal crystals diffracted to 2.8 Angstrom and were grown in the presence of double-stranded DNA. Monoclinic crystals were grown without DNA and diffracted to 3.2 Angstrom. Triclinic crystals were grown from a truncated apXPF protein lacking the tandem helix-hairpin-helix motifs and diffracted to 2.1 Angstrom.
机译:干皮病的眼点F组蛋白(XPF)的创始成员家庭3的皮瓣内切酶起着关键作用核苷酸切除修复,DNA复制和重组。Aeropyrum pernix,编码一个254 -残留的蛋白质(apXPF)。大肠杆菌和纯化的3色谱步骤。形式的apXPF生长在三方,单斜和三斜晶系的系统。衍射,至2.8埃,都在成长双链DNA的存在。晶体生长没有DNA和衍射3.2埃。截断apXPF蛋白质缺乏2.1 helix-hairpin-helix图案和衍射埃。

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