Expression, purification, crystallization and preliminary crystallographic study of the SRA domain of the human UHRF1 protein. - Archive ouverte HAL Access content directly
Journal Articles Acta crystallographica Section F : Structural biology communications [2014-...] Year : 2008

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

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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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inserm-00350743 , version 1 (03-02-2009)

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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 [2014-..], 2008, 64 (Pt 10), pp.922-5. ⟨10.1107/S1744309108027462⟩. ⟨inserm-00350743⟩
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