title: Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human transcription repressor ERH.
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 P3(1)21 or its enantiomorph P3(2)21, with unit-cell parameters a = b = 53.74, c = 67.45 A, alpha = beta = 90, gamma = 120 degrees. They diffract to at least 1.75 A. A selenomethionine derivative of the protein was prepared and crystallized for multiwavelength anomalous diffraction (MAD) phasing.
authors.affiliation: Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
authors.forename: Tengchuan
authors.initials: T
authors.lastname: Jin
authors.forename: Andrew
authors.initials: A
authors.lastname: Howard
authors.forename: Erica A
authors.initials: EA
authors.lastname: Golemis
authors.forename: Yingtong
authors.initials: Y
authors.lastname: Wang
authors.forename: Yu-Zhu
authors.initials: YZ
authors.lastname: Zhang
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D018797:Cell Cycle Proteins; C484495:ERH protein, human; D011994:Recombinant Proteins; D014157:Transcription Factors