Open AccessOverproduction, purification, crystallization and preliminary X‐ray diffraction studies of the human transcription repressor ERH
Author(s) -
Jin Tengchuan,
Howard Andrew,
Golemis Erica A.,
Wang Yingtong,
Zhang YuZhu
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105012388
Subject(s) - overproduction , repressor , crystallization , transcription (linguistics) , x ray , diffraction , crystallography , x ray crystallography , chemistry , transcription factor , materials science , gene , biochemistry , physics , optics , organic chemistry , linguistics , philosophy
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 P 3 1 21 or its enantiomorph P 3 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.