Crystallization and purification of the enzyme anthranilate phosphoribosyl transferase.
J Mol Biol
; 203(2): 523-4, 1988 Sep 20.
Article
em En
| MEDLINE
| ID: mdl-3199444
ABSTRACT
Anthranilate phosphoribosyl transferase from the bacterium Hafnia alvei has been crystallized. This enzyme is one of a small number that constitute the biosynthetic pathway for tryptophan. Large cubic crystals were grown at 4 degrees C by dialyzing away the glycerol from a protein solution that included ammonium sulfate, polyethylene glycol and glycerol. The crystals were much more temperature stable and resistant to X-ray deterioration than a previous, similar crystal form that had included glycerol. The crystals belong to the space group I432, a = b = c = 189 A (1 A = 0.1 nm). The ratio of the monomer molecular weight, 37,000, to the volume of the unit cell suggests that there is one homodimer per asymmetric unit. The crystals diffracted to a resolution of 3.0 A at the Stanford Synchotron Radiation Laboratory X-ray source.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pentosiltransferases
/
Antranilato Fosforribosiltransferase
/
Enterobacteriaceae
Idioma:
En
Ano de publicação:
1988
Tipo de documento:
Article