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Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

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

Member: Anastasia Gazi
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 24 Feb 2006

Fadouloglou VE, Kotsifaki D, Gazi AD, Fellas G, Meramveliotaki C, Deli A, Psylinakis E, Bouriotis V, Kokkinidis M

Link to Pubmed [PMID] – 16511317

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2006 Mar;62(Pt 3):261-4

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.