Crystallization and preliminary X-ray crystallographic studies of the thermoactive pullulanase type I, hydrolyzing alpha-1,6 glycosidic linkages, from Fervidobacterium pennivorans Ven5

Crystals of the thermoactive recombinant F. pennivorans type I pullulanase, purified from the supernatant of a Bacillus subtilis culture, have been ob tained by the vapour-diffusion method in the presence of the inhibitor beta -cyclodextrin (2 mM) by mixing protein (15 mg ml(-1)) with an equal volume of crystallization solution containing 0.1 M bis-tris propane pH 6.5, 50 m M MgCl2 and 15% polyethylene glycol 3350. Crystals diffracted to 3.0 Angstr om using conventional Cu K alpha radiation and belong to space group P2(1)2 (1)2(1), with unit-cell parameters a = 76.8, b = 96.2, c = 98.5 Angstrom. T he asymmetric unit contains one monomer. A preliminary 26% complete data se t has been collected at 2.2 Angstrom resolution using synchrotron radiation .