Purification, crystallization and preliminary characterization of a putative LmbE-like deacetylase from Bacillus cereus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):261-4. doi: 10.1107/S1744309106004660. Epub 2006 Feb 24.

Abstract

The Bacillus cereus BC1534 protein, a putative deacetylase from the LmbE family, has been purified to homogeneity and crystallized using the hanging-drop vapour-diffusion method. Crystals of the 26 kDa protein grown from MPD and acetate buffer belong to space group R32, with unit-cell parameters a = b = 76.7, c = 410.5 A (in the hexagonal setting). A complete native data set was collected to a resolution of 2.5 A from a single cryoprotected crystal using synchrotron radiation. As BC1534 shows significant sequence homology with an LmbE-like protein of known structure from Thermus thermophilus, molecular replacement will be used for crystal structure determination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / chemistry*
  • Amidohydrolases / isolation & purification*
  • Amino Acid Sequence
  • Bacillus cereus / chemistry*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification*
  • Crystallization / methods
  • Crystallography, X-Ray
  • Molecular Sequence Data

Substances

  • Bacterial Proteins
  • Amidohydrolases