Preliminary crystallographic analysis of trypanothione reductase from Crithidia fasciculata.
J Mol Biol
; 215(3): 335-7, 1990 Oct 05.
Article
em En
| MEDLINE
| ID: mdl-2231707
ABSTRACT
Trypanothione reductase, a flavoprotein disulfide reductase specific to trypanosomatid parasites, has been crystallized by vapor diffusion of a protein solution (10 mg/ml) against 22% polyethylene glycol (average Mr 8000) containing 100 mM-ammonium sulfate. Crystals of a size suitable for structure determination by X-ray diffraction have been obtained by seeding protein solutions with smaller crystals. The space-group is P21 (a = 60.9 A, b = 161.8 A, c = 58.4 A, beta = 99.1 degrees). The molecular mass and volume of the unit cell suggest that there is a dimer of the enzyme in the asymmetric unit, and this is confirmed by self-rotation functions calculated using data to 4.5 A resolution. The crystals diffract to beyond 3 A resolution. Crystals of another P21 form (a = 91.3 A, b = 114.4 A, c = 92.0 A, beta = 141.3 degrees) are observed to grow under similar conditions.
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Base de dados:
MEDLINE
Assunto principal:
Crithidia
/
NADH NADPH Oxirredutases
Limite:
Animals
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
1990
Tipo de documento:
Article