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

  • Fadouloglou V
  • Kotsifaki D
  • Gazi A
 et al. 
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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 ? (in the hexagonal setting). A complete native data set was collected to a resolution of 2.5 ? 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. ? 2006 International Union of Crystallography. All rights reserved.

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  • V.E. Fadouloglou

  • D. Kotsifaki

  • A.D. Gazi

  • G. Fellas

  • C. Meramveliotaki

  • A. Deli

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