Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human transcription repressor ERH
DOI: 10.1107/S1744309105012388
Additional Information
How to Cite
Jin, T., Howard, A., Golemis, E. A., Wang, Y. and Zhang, Y.-Z. (2005), Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human transcription repressor ERH. Acta Crystallographica Section F, 61: 531–533. doi: 10.1107/S1744309105012388
Keywords:
- transcription;
- pyrimidine biosynthesis;
- HNF1;
- PCD;
- DCoH.
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.
