Improvement of crystal quality by surface mutations of beta-lactamase Toho-1.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 65(Pt 4): 379-82, 2009 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-19342785
ABSTRACT
The beta-lactamase Toho-1 exhibits a strong tendency to form merohedrally twinned crystals. Here, the crystal quality of Toho-1 was improved by using surface modification to remove a sulfate ion involved in crystal packing. The surface-modified Toho-1 variant (R274N/R276N) was crystallized under similar conditions to those used for wild-type Toho-1. R274N/R276N did not form merohedrally twinned crystals. The crystals diffracted to a significantly higher resolution (approximately 0.97 A) than the wild-type crystals (1.65 A); they belonged to the same space group and had almost identical unit-cell parameters to those of wild-type Toho-1.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Beta-Lactamases
/
Proteínas de Escherichia coli
/
Mutação
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Japão