Crystallization and preliminary diffraction studies of a truncated form ofa novel protease from spores of Bacillus megaterium

During germination of spores of Bacillus species, a novel protease termed G PR initiates the degradation of a group of small acid-soluble spore protein s which protect the dormant spore's DNA from damage. Trypsin digestion of t he zymogen of B. megaterium GPR removes similar to 15 kDa from the C-termin al end of the 46 kDa zymogen subunit, leaving a 30 kDa subunit. Single crys tals of this truncated form of GPR have been obtained by the vapor-diffusio n method using PEG 4000 as a precipitating agent. The crystals belong to th e monoclinic space group P2(1), with unit-cell parameters a = 67.99, b = 10 5.34, c = 108.63 Angstrom, beta = 95.68 degrees. The cryofrozen crystals di ffract X-rays to about 3.3 Angstrom using synchrotron radiation.