Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme.
J Biochem
; 133(1): 29-32, 2003 Jan.
Article
em En
| MEDLINE
| ID: mdl-12761195
ABSTRACT
Lipocalin-type prostaglandin D synthase is the key enzyme for the production of prostaglandin D(2), a potent endogenous somnogen, in the brain. We cloned, produced, and crystallized the native enzyme and selenomethionyl Cys(65)Ala mutants of the recombinant mouse protein by the hanging drop vapor-diffusion method with both malonate and citrate as precipitants. The native crystals obtained with malonate belong to orthorhombic space group P2(1)2(1)2(1) with lattice constants a = 46.2, b = 66.8, and c = 105.3 A. The selenomethionyl crystals obtained with citrate belong to orthorhombic space group C222(1) with lattice constants a = 45.5, b = 66.8, and c = 104.5 A. The native crystals diffracted beyond 2.1 A resolution.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases Intramoleculares
Limite:
Animals
Idioma:
En
Revista:
J Biochem
Ano de publicação:
2003
Tipo de documento:
Article