Open AccessExpression, purification, crystallization and preliminary X‐ray studies of Lactobacillus jensenii enolase
Author(s) -
Harris Paul T.,
Raghunathan Kannan,
Spurbeck Rachel R.,
Arvidson Cindy G.,
Arvidson Dennis N.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110022748
Subject(s) - enolase , crystallization , microbiology and biotechnology , biology , biochemistry , chemistry , organic chemistry , immunology , immunohistochemistry
Recombinant Lactobacillus jensenii enolase fused to a C‐terminal noncleavable His tag was expressed in Escherichia coli , purified and crystallized by sitting‐drop vapor diffusion. A complete data set was collected to 3.25 Å resolution. The crystals belonged to space group I 4, with unit‐cell parameters a = b = 145.31, c = 99.79 Å. There were two protein subunits in the asymmetric unit, which gave a Matthews coefficient V M of 2.8 Å 3 Da −1 , corresponding to 55.2% solvent content.