与RhoC结合的mDia1的纯化与结晶
The purification and crystallization of mDia1 in complex with RhoC.
作者信息
Rose Rolf, Wittinghofer Alfred, Weyand Michael
机构信息
Department of Structural Biology, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):225-7. doi: 10.1107/S1744309105001065.
Abstract
An N-terminal construct of mouse mDia1 was recombinantly expressed in Escherichia coli, purified and crystallized in complex with truncated human RhoC using the hanging-drop vapour-diffusion method. Crystals were obtained using PEG 2K MME and MgSO4 as a precipitating agent and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 148.4, b = 85.2, c = 123.2 A. Complete native and SeMet-derivative data sets were collected at 100 K to 3.0 and 3.4 A resolution, respectively, using synchrotron radiation.
摘要
小鼠mDia1的N端构建体在大肠杆菌中重组表达，经纯化后，采用悬滴气相扩散法与截短的人RhoC形成复合物进行结晶。使用聚乙二醇2K甲氧基聚乙二醇（PEG 2K MME）和硫酸镁（MgSO4）作为沉淀剂获得晶体，晶体属于正交晶系空间群P2(1)2(1)2，晶胞参数a = 148.4，b = 85.2，c = 123.2 Å。分别使用同步辐射在100 K下收集完整的天然数据集和硒代甲硫氨酸（SeMet）衍生物数据集，分辨率分别为3.0 Å和3.4 Å。
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