Crystallization and preliminary X-ray studies of a protease from Pseudomonas aeruginosa.
A protease produced by Pseudomonas aeruginosa has been crystallized by the vapor-diffusion method using polyethylene glycol 4000 as a precipitant. The crystals belong to the hexagonal space group P6(1) (P6(5) with unit cell dimensions; a = b = 106.9 A, c = 96.9 A. There are two molecules per asymmetric unit. The crystals diffract X-rays to at least 3.0 A and are suitable for X-ray crystallographic studies.
Harada
S
S
Department of Applied Chemistry, Faculty of Engineering, Osaka University, Japan.
Nagara
A
A
Kurisu
G
G
Kai
Y
Y
D003460:Crystallization; D008666:Metalloendopeptidases / Q000737:chemistry*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D012697:Serine Endopeptidases / Q000737:chemistry*; D014961:X-Ray Diffraction
D012697:Serine Endopeptidases; C032923:microbial serine proteinases; D008666:Metalloendopeptidases