Shi Ning, Liu Yiwei, Ni Minghao, Yang MaoJun, Wu Jing, Peng Ying, Gao Feng, Sun Fei, Peng Xiaozhong, Qiang Boqin, Rao Zihe, Yuan Jiangang
National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Peking Union Medical College, National Human Genome Center, Beijing 100005, People's Republic of China.
Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):334-6. doi: 10.1107/S0907444903026696. Epub 2004 Jan 23.
The PTB domain of mouse dok1 fusion protein has been overexpressed in Escherichia coli and crystallized in a form suitable for X-ray crystallographic study. Crystals have been obtained using the vapour-diffusion method and belong to space group P2(1)2(1)2(1). X-ray diffraction data were collected in-house to 2.5 A resolution. A selenomethionine (SeMet) dok1 PTB fusion-protein derivative was expressed using the same expression system, purified in a reductive environment and crystals were obtained under similar conditions. Subsequently, three different wavelength data sets from the derivative crystal were collected to 2.5 A resolution at SPring-8.
小鼠dok1融合蛋白的PTB结构域已在大肠杆菌中过表达，并以适合X射线晶体学研究的形式结晶。使用气相扩散法获得了晶体，其属于空间群P2(1)2(1)2(1)。在内部收集了分辨率为2.5 Å的X射线衍射数据。使用相同的表达系统表达了硒代蛋氨酸（SeMet）dok1 PTB融合蛋白衍生物，在还原环境中进行纯化，并在类似条件下获得了晶体。随后，在SPring-8收集了来自衍生物晶体的三个不同波长的数据集，分辨率为2.5 Å。
