Expression, purification, crystallization and preliminary X-ray studies of Lactobacillus jensenii enolase

Journal Article · Thu Sep 02 00:00:00 EDT 2010 · Acta Crystallogr. F

DOI:https://doi.org/10.1107/S1744309110022748· OSTI ID:1002549

Harris, Paul T; Raghunathan, Kannan; Spurbeck, Rachel R; Arvidson, Cindy G; Arvidson, Dennis N ^[1]

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1. MSU

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 {angstrom} resolution. The crystals belonged to space group I4, with unit-cell parameters a = b = 145.31, c = 99.79 {angstrom}. There were two protein subunits in the asymmetric unit, which gave a Matthews coefficient V{sub M} of 2.8 {angstrom}{sup 3} Da{sup -1}, corresponding to 55.2% solvent content.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: USDOE
• OSTI ID: 1002549
• Journal Information: Acta Crystallogr. F, Vol. 66, Issue (8) ; 08, 2010
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
CRYSTALLIZATION
DIFFUSION
ESCHERICHIA COLI
LACTOBACILLUS
PROTEINS
PURIFICATION
RESOLUTION
SOLVENTS
SPACE GROUPS