Related Experiment Video
Updated: Jun 10, 2026
Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026
Expression, purification, crystallization and preliminary X-ray studies of Lactobacillus jensenii enolase
Paul T Harris1, Kannan Raghunathan, Rachel R Spurbeck
1Michigan State University, Department of Microbiology and Molecular Genetics and Michigan State University, Center for Microbial Pathogenesis, East Lansing, MI 48824, USA.
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.
