Author: Ramasubramanian Sundaramoorthy; Amanda L. Hughes; Hassane El-Mkami; David Norman; Tom Owen-Hughes
Title: Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome Document date: 2018_3_30
ID: ct2zhauz_52
Snippet: Xenopus H2B-K120 ubiquitinylated histones were refolded in equimolar ratios with H2A and similarly H3 K36 methyl analogue histones were refolded in equimolar ratios with histone H4 to obtain dimers and tetramers as described previously for wild type histones Dyer et al., and purified on a size exclusion chromatography using S200 gel filtation column. The peak fractions were analysed with SDS-PAGE gel and pooled. 601 DNA fragments of respective le.....
Document: Xenopus H2B-K120 ubiquitinylated histones were refolded in equimolar ratios with H2A and similarly H3 K36 methyl analogue histones were refolded in equimolar ratios with histone H4 to obtain dimers and tetramers as described previously for wild type histones Dyer et al., and purified on a size exclusion chromatography using S200 gel filtation column. The peak fractions were analysed with SDS-PAGE gel and pooled. 601 DNA fragments of respective lengths for recombinant nucleosome assembly were generated by PCR method as described previously (Sundaramoorthy et al., 2017) . Nucleosomes were generated by salt dialysis as described previously by combining H2A/H2B-K120 ubiquitin dimer, H3K36 methyl lysine analogue tetramer (2:1 ratio) with DNA containing PCR amplified Widom 601 DNA sequence.
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