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

Jing Li; Xiaojiao Xue; Jianbin Ruan; Minhao Wu; Zhiqiang Zhu; Jianye Zang

doi:10.1107/S1744309110016726

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 1;66(Pt 8):902-4. doi: 10.1107/S1744309110016726. Epub 2010 Jul 27.

Authors

Jing Li¹, Xiaojiao Xue, Jianbin Ruan, Minhao Wu, Zhiqiang Zhu, Jianye Zang

Affiliation

¹ School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cloning, Molecular
Crystallography
Crystallography, X-Ray
Histone Acetyltransferases / chemistry*
Histone Acetyltransferases / genetics
Histone Acetyltransferases / isolation & purification
Saccharomyces cerevisiae / chemistry*
Saccharomyces cerevisiae Proteins / chemistry*
Saccharomyces cerevisiae Proteins / genetics
Saccharomyces cerevisiae Proteins / isolation & purification
Tandem Repeat Sequences

Substances

Saccharomyces cerevisiae Proteins
Histone Acetyltransferases
Sgf29 protein, S cerevisiae