G3BP1 NTF2样结构域的纯化、结晶及初步X射线衍射分析
Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain.
作者信息
Vognsen Tina, Möller Ingvar Rúnar, Kristensen Ole
机构信息
Biostructural Research, Department of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):48-50. doi: 10.1107/S1744309110042156. Epub 2010 Dec 21.
Abstract
The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6 Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a=b=89.84, c=70.02 Å. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial phases were obtained by molecular replacement.
摘要
人G3BP1的核转运因子2样（NTF2样）结构域被亚克隆，在大肠杆菌中过表达并纯化。使用悬滴气相扩散法获得晶体。利用同步辐射将衍射数据收集至3.6 Å分辨率。晶体属于六方空间群P6(3)22，晶胞参数a = b = 89.84，c = 70.02 Å。每个不对称单元包含一个分子，估计溶剂含量为56%。通过分子置换获得初始相位。
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