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  • Title: Purification, crystallization and preliminary characterization of a putative LmbE-like deacetylase from Bacillus cereus.
    Author: Fadouloglou VE, Kotsifaki D, Gazi AD, Fellas G, Meramveliotaki C, Deli A, Psylinakis E, Bouriotis V, Kokkinidis M.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2006 Mar 01; 62(Pt 3):261-4. PubMed ID: 16511317.
    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.
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