Title : Crystallization of serine carboxypeptidases - Wilson_1990_J.Mol.Biol_211_301
Author(s) : Wilson KP , Liao DI , Bullock T , Remington SJ , Breddam K
Ref : Journal of Molecular Biology , 211 :301 , 1990
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.

PubMedSearch : Wilson_1990_J.Mol.Biol_211_301
PubMedID: 2308160
Gene_locus related to this paper: wheat-cbp02

Related information

Gene_locus wheat-cbp02

Citations formats

Wilson KP, Liao DI, Bullock T, Remington SJ, Breddam K (1990)
Crystallization of serine carboxypeptidases
Journal of Molecular Biology 211 :301

Wilson KP, Liao DI, Bullock T, Remington SJ, Breddam K (1990)
Journal of Molecular Biology 211 :301