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Expression, purification, crystallization and preliminary crystallographic study of the SRA domain of the human UHRF1 protein.

Abstract : Human UHRF1 belongs to the unique mammalian family of proteins which contain a SET- and RING finger-associated (SRA) domain. This 180-residue domain has been reported to play key roles in the functions of the protein. It allows UHRF1 to bind methylated DNA, histone deacetylase 1 and DNA methyltransferase 1, suggesting a bridge between DNA methylation and the histone code. No structural data is available for any SRA domain. Native and SeMet-labelled SRA domains of human UHRF1 were overexpressed in Escherichia coli cells, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion method. A complete MAD data set was collected to 2.2 A resolution at 100 K. Crystals of the SeMet-labelled protein belonged to the trigonal space group P3(2)21, with unit-cell parameters a = b = 53.78, c = 162.05 A.
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Submitted on : Tuesday, February 3, 2009 - 3:47:22 PM
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Bénédicte Delagoutte, Nada Lallous, Catherine Birck, Pierre Oudet, Jean Pierre Samama. Expression, purification, crystallization and preliminary crystallographic study of the SRA domain of the human UHRF1 protein.. Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd,, 2008, 64 (Pt 10), pp.922-5. ⟨10.1107/S1744309108027462⟩. ⟨inserm-00350743⟩

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