Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae.
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.
Sack
S
S
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany.
Dauter
Z
Z
Wanke
C
C
Amrhein
N
N
Mandelkow
E
E
Schönbrunn
E
E
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*
D011994:Recombinant Proteins; D014166:Transferases; D019883:Alkyl and Aryl Transferases; C022566:UDP-N-acetylglucosamine 1-carboxyvinyltransferase