Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus.
Acta Crystallogr D Biol Crystallogr
; 56(Pt 7): 900-1, 2000 Jul.
Article
em En
| MEDLINE
| ID: mdl-10930838
ABSTRACT
An esterase from the hyperthermophilic archeon Archaeoglobus fulgidus has been expressed, purified and crystallized in a form suitable for structure analysis. The enzyme has a molecular mass of 35 467 Da and shows sequence similarity to other esterases known to possess the alpha/beta hydrolase fold. The crystals diffract to 2.8 A and belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 A.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Archaeoglobus fulgidus
/
Esterases
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Austrália