Purification, crystallization and preliminary characterization of a putative LmbE-like deacetylase from Bacillus cereus.
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.
Fadouloglou
Vasiliki E
VE
Department of Biology, University of Crete, PO Box 2208, GR-71409 Heraklion, Crete, Greece.
Kotsifaki
Dina
D
Gazi
Anastasia D
AD
Fellas
Georgios
G
Meramveliotaki
Chrysi
C
Deli
Alexandra
A
Psylinakis
Emmanuel
E
Bouriotis
Vassilis
V
Kokkinidis
Michael
M
D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D000581:Amidohydrolases