title: Expression, purification, crystallization and preliminary X-ray studies of Lactobacillus jensenii enolase.
abstract: 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 A resolution. The crystals belonged to space group I4, with unit-cell parameters a=b=145.31, c=99.79 A. There were two protein subunits in the asymmetric unit, which gave a Matthews coefficient VM of 2.8 A3 Da(-1), corresponding to 55.2% solvent content.
authors.affiliation: Michigan State University, Department of Microbiology and Molecular Genetics and Michigan State University, Center for Microbial Pathogenesis, East Lansing, MI 48824, USA.
authors.forename: Paul T
authors.initials: PT
authors.lastname: Harris
authors.forename: Kannan
authors.initials: K
authors.lastname: Raghunathan
authors.forename: Rachel R
authors.initials: RR
authors.lastname: Spurbeck
authors.forename: Cindy G
authors.initials: CG
authors.lastname: Arvidson
authors.forename: Dennis N
authors.initials: DN
authors.lastname: Arvidson
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D007778:Lactobacillus / Q000201:enzymology*; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D010751:Phosphopyruvate Hydratase