Crystallization and preliminary crystallographic analysis of carboxypeptidase G2 from Pseudomonas sp. strain RS-16.
Carboxypeptidase G2, a zinc metalloenzyme isolated from Pseudomonas sp. strain RS-16, which catalyses the hydrolytic cleavage of reduced and non-reduced folates to pteroates and L-glutamate, has been crystallized from polyethylene glycol (average Mr 4000) by vapour diffusion. The crystal symmetry is monoclinic C2, with unit cell dimensions a = 206 A, b = 82 A, c = 116 A and beta = 118 degrees. The molecular mass and volume of the unit cell suggest that there are two dimers of the enzyme in the asymmetric unit. The crystals diffract to at least 3.0 A and are suitable for X-ray structure analysis.
Lloyd
L F
LF
Blackett Laboratory, Imperial College, London, U.K.
Collyer
C A
CA
Sherwood
R F
RF
D046911:Macromolecular Substances; D008970:Molecular Weight; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*; D014961:X-Ray Diffraction / Q000379:methods; D011623:gamma-Glutamyl Hydrolase / Q000737:chemistry* / Q000302:isolation & purification
D046911:Macromolecular Substances; D011623:gamma-Glutamyl Hydrolase