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Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human transcription repressor ERH

Journal Article · · Acta Crystallographica. Section F
;  [1];  [2]; ;  [1]
  1. Department of Biology, Illinois Institute of Technology, Chicago, IL 60616 (United States)
  2. Fox Chase Cancer Center, Philadelphia, PA 19111 (United States)
Crystallization of human enhancer of rudimentary homologue protein. 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 P3{sub 1}21 or its enantiomorph P3{sub 2}21, 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.
OSTI ID:
22356002
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English