title: Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae.
abstract: Single crystals of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae have been grown by vapor diffusion using phosphate buffer as the precipitant. The crystals belong to the monoclinic space group C2 with a = 86.9 A, b = 155.9 A, c = 83.8 A, beta = 91.6 degrees. Assuming two monomers per asymmetric unit, the solvent content of these crystals is 63%. Flash-frozen crystals diffract to beyond 2 A resolution.
authors.affiliation: Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Sack
authors.forename: Z
authors.initials: Z
authors.lastname: Dauter
authors.forename: C
authors.initials: C
authors.lastname: Wanke
authors.forename: N
authors.initials: N
authors.lastname: Amrhein
authors.forename: E
authors.initials: E
authors.lastname: Mandelkow
authors.forename: E
authors.initials: E
authors.lastname: Schönbrunn
mesh_terms: D019883:Alkyl and Aryl Transferases; D003460:Crystallization; D018360:Crystallography, X-Ray; D016972:Enterobacter cloacae / Q000201:enzymology*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D014166:Transferases / Q000737:chemistry*
chemical_list: D011994:Recombinant Proteins; D014166:Transferases; D019883:Alkyl and Aryl Transferases; C022566:UDP-N-acetylglucosamine 1-carboxyvinyltransferase