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

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

Jing Li  1 , Xiaojiao Xue, Jianbin Ruan, Minhao Wu, Zhiqiang Zhu, Jianye Zang
Affiliations

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

Jing Li et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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.

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Figures

Figure 1
Figure 1
Crystal of MBP-Sgf29.
Figure 2
Figure 2
X-ray diffraction image collected from the crystal of MBP-Sgf29.
See this image and copyright information in PMC

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