Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of SET/TAF-Iß δN from Homo sapiens.
The histone chaperone SET encoded by the SET gene, which is also known as template-activating factor Iß (TAF-Iß), is a multifunctional molecule that is involved in many biological phenomena such as histone binding, nucleosome assembly, chromatin remodelling, replication, transcription and apoptosis. A truncated SET/TAF-Iß ΔN protein that lacked the first 22 residues of the N-terminus but contained the C-terminal acidic domain and an additional His6 tag at the C-terminus was overexpressed in Escherichia coli and crystallized by the hanging-drop vapour-diffusion method using sodium acetate as precipitant at 283 K. The crystals diffracted to 2.7 A resolution and belonged to space group P4(3)2(1)2.
Xu
Zhen
Z
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
Yang
Weili
W
Shi
Nuo
N
Gao
Yongxiang
Y
Teng
Maikun
M
Niu
Liwen
L
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D056488:Histone Chaperones / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D006801:Humans; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D004268:DNA-Binding Proteins; D056488:Histone Chaperones; C513473:SET protein, human; D014157:Transcription Factors