Crystallization and preliminary diffraction studies of a truncated form of a novel protease from spores of Bacillus megaterium.
During germination of spores of Bacillus species, a novel protease termed GPR initiates the degradation of a group of small acid-soluble spore proteins which protect the dormant spore's DNA from damage. Trypsin digestion of the zymogen of B. megaterium GPR removes approximately 15 kDa from the C-terminal end of the 46 kDa zymogen subunit, leaving a 30 kDa subunit. Single crystals of this truncated form of GPR have been obtained by the vapor-diffusion method using PEG 4000 as a precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 67.99, b = 105.34, c = 108.63 A, beta = 95.68 degrees. The cryofrozen crystals diffract X-rays to about 3.3 A using synchrotron radiation.
Ponnuraj
K
K
Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
Kelly
S
S
Nessi
C
C
Setlow
P
P
Jedrzejas
M J
MJ
D001410:Bacillus megaterium / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification*; D008970:Molecular Weight; D012808:Sigma Factor; D013171:Spores, Bacterial / Q000201:enzymology; D014157:Transcription Factors; D014357:Trypsin
D001426:Bacterial Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C092468:spoIIR protein, Bacillus subtilis; C030069:spore-specific proteins, Bacillus; D010450:Endopeptidases; D014357:Trypsin