酿酒酵母Sgf29串联 Tudor 结构域的克隆、纯化、结晶及初步晶体学分析。
Cloning, purification, crystallization and preliminary crystallographic analysis of the tandem tudor domain of Sgf29 from Saccharomyces cerevisiae.
作者信息
Li Jing, Xue Xiaojiao, Ruan Jianbin, Wu Minhao, Zhu Zhiqiang, Zang Jianye
机构信息
School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt 8):902-4. doi: 10.1107/S1744309110016726. Epub 2010 Jul 27.
Abstract
The protein Sgf29 has been identified as a subunit of the SAGA (Spt-Ada-Gcn5 acetyltransferase) histone acetyltransferase complex in Saccharomyces cerevisiae, which is conserved from yeast to humans. The tandem tudor domain at the C-terminus of Sgf29 was crystallized using the hanging-drop vapour-diffusion method and the crystals diffracted to 1.92 A resolution. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a=49.76, b=95.10, c=114.43 A, and are estimated to contain one protein molecule per asymmetric unit.
摘要
蛋白质Sgf29已被鉴定为酿酒酵母中SAGA（Spt-Ada-Gcn5乙酰转移酶）组蛋白乙酰转移酶复合物的一个亚基，该复合物从酵母到人类都保守。使用悬滴气相扩散法对Sgf29 C端的串联 Tudor 结构域进行了结晶，晶体衍射分辨率达到1.92 Å。晶体属于空间群P2(1)2(1)2(1)，晶胞参数a = 49.76、b = 95.10、c = 114.43 Å，估计每个不对称单元包含一个蛋白质分子。
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