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Updated: Aug 25, 2026

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Expression, purification, crystallization and preliminary crystallographic studies of the Enterococcus faecalis
Adelia Razeto1, Karin Giller, Wolfgang Haas
1Department for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Abstract:
The expression of an exotoxin called cytolysin contributes to the virulence of Enterococcus faecalis, one of the organisms responsible for antibiotic resistant infections acquired in hospitals. The DNA-binding protein CylR2 is a transcriptional repressor of cytolysin. At a specific cell density, cytolysin triggers signaling events, which result in the dissociation of CylR2 from its DNA-binding site. CylR2 was overexpressed in Escherichia coli and purified and crystals diffracting to 1.9 A were obtained in two different crystal forms. One crystal form belongs to space group P4(1), with unit-cell parameters a = 63.7, b = 63.7, c = 41.2 A, alpha = beta = gamma = 90 degrees, and the other belongs to space group P1, with unit-cell parameters a = 36.9, b = 45.0, c = 47.7 A, alpha = 67, beta = 90, gamma = 66 degrees.

