Cloning, purification, crystallization and preliminary crystallographic analysis of the tandem tudor domain of Sgf29 from Saccharomyces cerevisiae.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.2010 Aug 01;66(Pt 8):902-4. Epub 2010 Jul 27
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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.
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基因功能
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原始数据
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文献解读
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