Cloning, purification, crystallization and preliminary crystallographic analysis of the tandem tudor domain of Sgf29 from Saccharomyces cerevisiae.
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.
Li
Jing
J
School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.
Xue
Xiaojiao
X
Ruan
Jianbin
J
Wu
Minhao
M
Zhu
Zhiqiang
Z
Zang
Jianye
J
D003001:Cloning, Molecular; D003461:Crystallography; D018360:Crystallography, X-Ray; D051548:Histone Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D020080:Tandem Repeat Sequences
D029701:Saccharomyces cerevisiae Proteins; D051548:Histone Acetyltransferases; C553425:Sgf29 protein, S cerevisiae