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 language | English |
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Pages (from-to) | 531-533 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 61 |
Issue number | 5 |
DOIs | |
State | Published - 2005 |
Keywords
- Cell Cycle Proteins/chemistry
- Cloning, Molecular
- Crystallization
- Escherichia coli/genetics
- Humans
- Recombinant Proteins/genetics
- Transcription Factors/chemistry
- X-Ray Diffraction