Crystallization of serine carboxypeptidases.

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(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.

journal_name

J Mol Biol

authors

Wilson KP,Liao DI,Bullock T,Remington SJ,Breddam K

doi

10.1016/0022-2836(90)90352-m

subject

Has Abstract

pub_date

1990-01-20 00:00:00

pages

301-3

issue

2

eissn

0022-2836

issn

1089-8638

pii

0022-2836(90)90352-M

journal_volume

211

pub_type

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