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Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of SET/TAF-Iß ?N from Homo sapiens.

ABSTRACT: 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 ?N 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.

SUBMITTER: Xu Z

PROVIDER: S-EPMC2917293 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of SET/TAF-Iß δN from Homo sapiens.

Xu Zhen Z Yang Weili W Shi Nuo N Gao Yongxiang Y Teng Maikun M Niu Liwen L

Acta crystallographica. Section F, Structural biology and crystallization communications 20100729 Pt 8

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 Esch ...[more]

PMID: 20693670

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