Crystallization of serine carboxypeptidases.
Crystallization of three different serine carboxypeptidases has been achieved by the method of hanging-drop vapor diffusion. Serine carboxypeptidases II from wheat bran and malted barley crystallize isomorphously from polyethylene glycol solutions at room temperature (pH 4 to 7) in space group P4(1)2(1)2 or enantiomorph with cell dimensions of a = b = 98.2 A and c = 209.5 A. The crystals diffract to about 2.3 A resolution using rotating-anode X-ray generators. Assuming a dimer of Mr 120,000 in the asymmetric unit, Vm = 2.1 A3/dalton. These crystals appear suitable for structural studies. A genetically engineered serine carboxypeptidase from yeast, which lacks three of four glycosylation sites present in the wild-type, has also been crystallized by vapor diffusion against methylpentanediol at 4 degrees C, pH 6.4 to 8.0.
Wilson
K P
KP
Institute of Molecular Biology, University of Oregon, Eugene 97403.
Liao
D I
DI
Bullock
T
T
Remington
S J
SJ
Breddam
K
K
D002268:Carboxypeptidases / Q000302:isolation & purification*; D003460:Crystallization; D007202:Indicators and Reagents; D012697:Serine Endopeptidases / Q000302:isolation & purification*
D007202:Indicators and Reagents; D002268:Carboxypeptidases; D012697:Serine Endopeptidases