哺乳动物翻译延伸因子eEF1A2的纯化、结晶及初步X射线晶体学分析。
Purification, crystallization and preliminary X-ray crystallographic analysis of mammalian translation elongation factor eEF1A2.
作者信息
Yaremchuk A, Shalak V F, Novosylna O V, Negrutskii B S, Crépin T, El'skaya A V, Tukalo M
机构信息
State Key Laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo Street, 03680 Kyiv-143, Ukraine.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):295-7. doi: 10.1107/S1744309112000243. Epub 2012 Feb 22.
Abstract
Translation elongation factor eEF1A2 was purified to homogeneity from rabbit muscle by two consecutive ion-exchange column-chromatography steps and this mammalian eEF1A2 was successfully crystallized for the first time. Protein crystals obtained using ammonium sulfate as precipitant diffracted to 2.5 Å resolution and belonged to space group P6(1)22 or P6(3)22 (unit-cell parameters a = b = 135.4, c = 304.6 Å). A complete native data set was collected to 2.7 Å resolution.
摘要
通过连续两步离子交换柱色谱法从兔肌肉中纯化得到了均一的翻译延伸因子eEF1A2，并且首次成功地使这种哺乳动物的eEF1A2结晶。以硫酸铵作为沉淀剂获得的蛋白质晶体衍射分辨率达到2.5 Å，属于空间群P6(1)22或P6(3)22（晶胞参数a = b = 135.4，c = 304.6 Å）。收集了一个完整的天然数据集，分辨率达到2.7 Å。
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