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

Tengchuan Jin, Andrew Howard, Erica A. Golemis, Yingtong Wang, Yu Zhu Zhang

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish
Pages (from-to)531-533
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number5
DOIs
StatePublished - 2005

Keywords

  • Cell Cycle Proteins/chemistry
  • Cloning, Molecular
  • Crystallization
  • Escherichia coli/genetics
  • Humans
  • Recombinant Proteins/genetics
  • Transcription Factors/chemistry
  • X-Ray Diffraction

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