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 Bioljournal_title
Journal of molecular biologyauthors
Wilson KP,Liao DI,Bullock T,Remington SJ,Breddam Kdoi
10.1016/0022-2836(90)90352-msubject
Has Abstractpub_date
1990-01-20 00:00:00pages
301-3issue
2eissn
0022-2836issn
1089-8638pii
0022-2836(90)90352-Mjournal_volume
211pub_type
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