Differential effects of short affinity tags on the crystallization of Pyrococcus furiosus maltodextrin-binding protein.
Acta Crystallogr D Biol Crystallogr
; 58(Pt 3): 392-7, 2002 Mar.
Article
en En
| MEDLINE
| ID: mdl-11856823
ABSTRACT
Pyrococcus furiosus maltodextrin-binding protein readily forms large orthorhombic crystals that diffract to high resolution. This protein was used as a model system to investigate the influence of five short affinity tags (His(6), Arg(5), Strep tag II, FLAG tag and the biotin acceptor peptide) on the formation of protein crystals and their ability to diffract X-rays. The results indicate that the amino-acid sequence of the tag can have a profound effect on both of these parameters. Consequently, the ability to obtain diffracting crystals of a particular protein may depend as much on which affinity tag is selected as it does on whether an affinity tag is used at all.
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Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Proteínas Portadoras
/
Pyrococcus furiosus
/
Proteínas de Escherichia coli
Idioma:
En
Año:
2002
Tipo del documento:
Article