Work

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

Year: 2005

Type: article

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.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309105012388

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

Institutions: Illinois Institute of Technology, Fox Chase Cancer Center

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

OpenAlex ID: W1994828186

FWCI: 0.606

Cites: 10

Cited by: 6

Related to: 10