Purification, crystallization and preliminary X-ray diffraction analysis of human Gadd45γ

被引:0
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作者
Zhang, Wenzheng [1 ,2 ,3 ,4 ]
Zhao, Mingzhuo [5 ]
Li, Jianhui [1 ]
Li, Xuemei [1 ]
Zeng, ZongHao [1 ]
Rao, Zihe [1 ,2 ,3 ,4 ]
机构
[1] Chinese Acad Sci, Inst Biophys, Nat Lab Biomacromol, Beijing 100101, Peoples R China
[2] Tsinghua Univ, Struct Biol Lab, Beijing 100084, Peoples R China
[3] Nankai Univ, Coll Life Sci, Tianjin 300071, Peoples R China
[4] Nankai Univ, Tianjin State Lab Prot Sci, Tianjin 300071, Peoples R China
[5] Hunan Univ Sci & Technol, Sch Phys, Xiangtan 411201, Peoples R China
关键词
D O I
10.1107/S174430910803306X
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Gadd45, MyD118 and CR6 (also termed Gadd45 alpha, Gadd45 beta and Gadd45 gamma, respectively) comprise a family of proteins that play important roles in negative growth control, maintenance of genomic stability, DNA repair, cell-cycle control and apoptosis. Recombinant human Gadd45 gamma and its selenomethionine derivative were expressed in an Escherichia coli expression system and purified; they were then crystallized using the hanging-drop vapour-diffusion method. Diffraction-quality crystals were grown at 291 K using PEG 3350 as precipitant. Using synchrotron radiation, the best diffraction data were collected to 2.3 angstrom resolution for native crystals at 100 K; selenomethionyl derivative data were collected to 3.3 angstrom resolution. All the crystals belonged to space group I2(1)3, with approximate unit-cell parameters a = b = c = 126 angstrom
引用
收藏
页码:1070 / 1073
页数:4
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