| Literature DB >> 16511317 |
Vasiliki E Fadouloglou1, Dina Kotsifaki, Anastasia D Gazi, Georgios Fellas, Chrysi Meramveliotaki, Alexandra Deli, Emmanuel Psylinakis, Vassilis Bouriotis, Michael Kokkinidis.
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.Entities:
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Year: 2006 PMID： 16511317 PMCID： PMC2197166 DOI： 10.1107/S1744309106004660
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091