Initiating a crystallographic study of UDP-galactopyranose mutase from Escherichia coli

Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):399-402. doi: 10.1107/s0907444998010877.


UDP-galactopyranose mutase, the enzyme responsible for the conversion of UDP-galactopyranose to UDP-galactofuranose, has been crystallized in a form suitable for X-ray diffraction studies. UDP-galactofuranose is a key component of mycobacterial cell walls. Crystals of both the native protein and a selenomethionine variant have been grown by the vapour-diffusion method in hanging drops, and diffract to beyond 3.0 A using synchrotron radiation. Equilibration was against a solution of 20%(w/v) polyethylene glycol (4K), 12%(v/v) 2--propanol, 0.1 M HEPES pH 7.6 at 293.5 K. Crystals grow as thin plates of dimensions 0.4 x 0.2 x approximately 0.02 mm. They are monoclinic [corrected], space group P21, with unit-cell dimensions a = 71. 12, b = 58.42, c = 96.38 A, beta = 96.38 degrees. 92% (native) and 94% (selenomethionine) complete data sets have been recorded to 2.9 A (Rmerge = 5.0%) and 3.0 A (Rmerge = 6.9%), respectively. The Matthews coefficient is 2.35 A3 Da-1 for a dimer in the asymmetric unit, the solvent content being 47%. Diffraction data have also been recorded on a putative platinum derivative to 3.5 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins*
  • Intramolecular Transferases / chemistry*
  • Intramolecular Transferases / isolation & purification
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Homology, Amino Acid


  • Escherichia coli Proteins
  • Intramolecular Transferases
  • Glf protein, E coli
  • UDP-galactopyranose mutase