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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray analysis of the conserved domain IV of Escherichia coli 4.5S RNA
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Crystallization and preliminary X-ray analysis of the conserved domain IV of Escherichia coli 4.5S RNA

机译：结晶和初步的x射线分析大肠杆菌的保守域四4.5 sRNA

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摘要

4.5S RNA forms with Ffh protein the prokaryotic signal recognition particle (SRP), a highly conserved ribonucleoprotein complex essential for protein secretion. It also independently binds to elongation factor G (EF-G) in the ribosome and has a function in a subset of translocation events that is transient but required for viability. Crystals of three different constructs encompassing the conserved domain IV of 4.5S RNA, containing the recognition elements for both Ffh and EF-G, were obtained. Native X-ray diffraction data were collected for two crystal forms under cryogenic cooling conditions. The best crystals are of a 45 nt construct, diffract anisotropically to 2.6 A resolution using synchrotron radiation and belong to space group P3_221, with unit-cell parameters a = b = 69.1, c = 84.6 A and a single RNA molecule per asymmetric unit.
机译：4.5 s RNA形式Ffh蛋白质的原核信号识别颗粒(SRP),一个高度守恒的核糖核蛋白复合体必不可少的蛋白质的分泌。延长因子G (EF-G)核糖体有一个功能的一个子集易位吗瞬态,但所需的事件生存能力。包括4.5 s RNA的保守域四世,对Ffh包含识别元素和EF-G。数据收集了两种晶体形式低温冷却条件。衍射,45元的构造吗anisotropically 2.6解决方案使用同步加速器辐射,属于空间群P3_221,晶胞参数a = b = 69.1, c= 84.6和一个RNA分子不对称单位。

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