SGD Paper 
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Li J, et al. (2010) 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 66(Pt 8):902-4
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.
| Status: Published | Type: Journal Article | PubMed ID: 20693663 |
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| Topics | Genes linked to topics |
|---|---|
| SGF29 | |
| Additional Literature |  |
| Protein Physical Properties | |
| Protein/Nucleic Acid Structure | |
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