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- W1994828186 abstract "The human gene coding for the enhancer of rudimentary homologue (ERH) protein was overexpressed in Escherichia coli. The ERH protein was purified by anion-exchange, hydrophobic interaction and gel-filtration chromatography. Well diffracting single crystals were obtained by the vapour-diffusion method in hanging drops. The crystals belong to the trigonal space group P3121 or its enantiomorph P3221, with unit-cell parameters a = b = 53.74, c = 67.45 Å, α = β = 90, γ = 120°. They diffract to at least 1.75 Å. A selenomethionine derivative of the protein was prepared and crystallized for multiwavelength anomalous diffraction (MAD) phasing." @default.
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- W1994828186 date "2005-04-28" @default.
- W1994828186 modified "2023-09-25" @default.
- W1994828186 title "Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human transcription repressor ERH" @default.
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- W1994828186 doi "https://doi.org/10.1107/s1744309105012388" @default.
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