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本文引用的文献

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Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
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Structure and function of histone methylation binding proteins.组蛋白甲基化结合蛋白的结构与功能
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Histone acetyltransferase complexes: one size doesn't fit all.组蛋白乙酰转移酶复合物：并非一概而论。
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Multi-tasking on chromatin with the SAGA coactivator complexes.利用SAGA共激活因子复合体在染色质上进行多任务处理。
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Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc.TFTC/STAGA组蛋白乙酰转移酶复合物的一种新成分大鼠SGF29在肝细胞癌中的表达失调：对c-Myc致癌潜力的可能影响。
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Chromatin modifications and their function.染色质修饰及其功能。
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The diverse functions of histone lysine methylation.组蛋白赖氨酸甲基化的多种功能。
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8
Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry.真核生物转录机制的蛋白质组学：通过多维质谱法鉴定与酵母TFIID组分相关的蛋白质。
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9
Expanded lysine acetylation specificity of Gcn5 in native complexes.Gcn5在天然复合物中赖氨酸乙酰化特异性的扩展
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Solvent content of protein crystals.蛋白质晶体的溶剂含量。
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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.

DOI:10.1107/S1744309110016726
PMID:20693663
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2917286/
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。