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Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography
E. Boura, A. Baumlova, D. Chalupska, A. Dubankova, M. Klima,
Language English Country United States
Document type Journal Article
NLK
Free Medical Journals
from 1992 to 1 year ago
PubMed Central
from 1992 to 1 year ago
Europe PubMed Central
from 1992 to 1 year ago
Medline Complete (EBSCOhost)
from 2010-01-01 to 1 year ago
Wiley Free Content
from 1996 to 1 year ago
PubMed
28342173
DOI
10.1002/pro.3162
Knihovny.cz E-resources
- MeSH
- Bacteriophage T4 * enzymology genetics MeSH
- Chromatography, Affinity methods MeSH
- Crystallography, X-Ray methods MeSH
- Muramidase * chemistry genetics isolation & purification MeSH
- Mutation * MeSH
- Publication type
- Journal Article MeSH
Phage T4 lysozyme is a well folded and highly soluble protein that is widely used as an insertion tag to improve solubility and crystallization properties of poorly behaved recombinant proteins. It has been used in the fusion protein strategy to facilitate crystallization of various proteins including multiple G protein-coupled receptors, lipid kinases, or sterol binding proteins. Here, we present a structural and biochemical characterization of its novel, metal ions-binding mutant (mbT4L). We demonstrate that mbT4L can be used as a purification tag in the immobilized-metal affinity chromatography and that, in many respects, it is superior to the conventional hexahistidine tag. In addition, structural characterization of mbT4L suggests that mbT4L can be used as a purification tag compatible with X-ray crystallography.
References provided by Crossref.org
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