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

<jats:p>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 Å using synchrotron radiation. Equilibration was against a solution of 20%(<jats:italic>w</jats:italic>/<jats:italic>v</jats:italic>) polyethylene glycol (4K), 12%(<jats:italic>v</jats:italic>/<jats:italic>v</jats:italic>) 2-propanol, 0.1 <jats:italic>M</jats:italic> HEPES pH 7.6 at 293.5 K. Crystals grow as thin plates of dimensions 0.4 × 0.2 × ∼0.02 mm. They are orthorhombic, space group <jats:italic>P</jats:italic>2<jats:sub>1</jats:sub>, with unit-cell dimensions <jats:italic>a</jats:italic> = 71.12, <jats:italic>b</jats:italic> = 58.42, <jats:italic>c</jats:italic> = 96.38 Å, β = 96.38°. 92% (native) and 94% (selenomethionine) complete data sets have been recorded to 2.9 Å (<jats:italic>R</jats:italic> <jats:sub>merge</jats:sub> = 5.0%) and 3.0 Å (<jats:italic>R</jats:italic> <jats:sub>merge</jats:sub> = 6.9%), respectively. The Matthews coefficient is 2.35 Å<jats:sup>3</jats:sup> Da<jats:sup>−1</jats:sup> 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 Å.</jats:p>