Crystallization and preliminary X-ray diffraction analysis of the putative aldose 1-epimerase YeaD from Escherichia coli

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt 8):951-3. doi: 10.1107/S1744309110024140. Epub 2010 Jul 29.

Abstract

Escherichia coli YeaD (ecYeaD) is suggested to be a member of the galactose mutarotase-like superfamily. Galactose mutarotase is an enzyme that converts alpha-galactose to beta-galactose. The known structures of these galactose mutarotase-like proteins are similar to those of galactose mutarotases, with the catalytic residues being conserved, but there are some differences between them in the substrate-binding pocket. In order to reveal the specificity of ecYeaD, a three-dimensional structure is essential. Full-length ecYeaD with an additional 6xHis tag at the C-terminus was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 4000 as a precipitant at 283 K. An X-ray diffraction data set was collected to a resolution of 1.9 A from a single flash-cooled crystal that belonged to space group P2(1)2(1)2(1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Epimerases / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*

Substances

  • Carbohydrate Epimerases
  • aldose 1-epimerase