title: Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis.
abstract: The gene product of open reading frame Rv1018c from Mycobacterium tuberculosis is annotated as encoding a probable N-acetylglucosamine 1-phosphate uridylyltransferase (MtbGlmU), an enzyme that catalyzes the biosynthesis of UDP-N-acetylglucosamine, a precursor common to lipopolysaccharide and peptidoglycan biosynthesis. Following overexpression in Escherichia coli, the enzyme was purified and crystallized using the hanging-drop vapour-diffusion method. Native diffraction data were collected from crystals belonging to space group R32 and processed to a resolution of 2.2 A.
authors.affiliation: Protein Structure and Function Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
authors.forename: Jiang
authors.initials: J
authors.lastname: Yin
authors.forename: Craig R
authors.initials: CR
authors.lastname: Garen
authors.forename: Maia M
authors.initials: MM
authors.lastname: Cherney
authors.forename: Leonid T
authors.initials: LT
authors.lastname: Cherney
authors.forename: Michael N G
authors.initials: MN
authors.lastname: James