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Crystallographic studies on D-amino acid oxidase.

Authors :
Bolognesi M
Ungaretti L
Curti B
Ronchi S
Source :
The Journal of biological chemistry [J Biol Chem] 1978 Oct 25; Vol. 253 (20), pp. 7513-4.
Publication Year :
1978

Abstract

D-amino acid oxidase, a flavoprotein from hog kidneys, has been crystalized in two different forms. Orthorhombic prisms have been obtained from the enzyme.benzoate complex at pH 8.3; the space group is C2221 and the cell dimensions are a = 325A, b = 138.8 A, c = 200 A. At lower pH values, the enzyme crystallizes in trigonal prisms with a = b = 116.0 A, c = 399 A, space group P3112 or its enantiomorph. The two crystal forms have been obtained at 28 degrees C while at 4 degrees C only weak evidence of crystallization has been detected. In both crystalline modifications, the protein is highly associated.

Details

Language :
English
ISSN :
0021-9258
Volume :
253
Issue :
20
Database :
MEDLINE
Journal :
The Journal of biological chemistry
Publication Type :
Academic Journal
Accession number :
29898