Cloning, purification, crystallization and preliminary crystallographic analysis of the tandem tudor domain of Sgf29 from Saccharomyces cerevisiae

被引：2
|
作者：
Xu, Zhen [1 ,2 ,3 ]
Yang, Weili [1 ,2 ,3 ]
Shi, Nuo [1 ,2 ,3 ]
Gao, Yongxiang [1 ,2 ,3 ]
Teng, Maikun [1 ,2 ,3 ]
Niu, Liwen [1 ,2 ,3 ]
机构：
[1] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China
[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui, Peoples R China
[3] Chinese Acad Sci, Key Lab Struct Biol, Hefei 230026, Anhui, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词：
Sgf29; Saccharomyces cerevisiae; tudor domains; ACTIVATING FACTOR-I; REPLICATION FACTOR; ADENOVIRUS GENOME; TRANSCRIPTION; SET; DNA; ACETYLATION;
D O I：
10.1107/S1744309110021779
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：926 / 928
页数：3
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