Abstract
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 12 12 or enantiomorph with cell dimensions of a = b = 98.2 A ̊ and c = 209.5 A ̊ . The crystals diffract to about 2.3 Å resolution using rotating-anode X-ray generators. Assuming a dimer of M r 120,000 in the asymmetric unit, V m = 2.1 A ̊ 3/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 °C, pH 6.4 to 8.0.
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