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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,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články
NLK
Free Medical Journals
od 1992 do Před 1 rokem
PubMed Central
od 1992 do Před 1 rokem
Europe PubMed Central
od 1992 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2010-01-01 do Před 1 rokem
Wiley Free Content
od 1996 do Před 1 rokem
PubMed
28342173
DOI
10.1002/pro.3162
Knihovny.cz E-zdroje
- MeSH
- bakteriofág T4 * enzymologie genetika MeSH
- chromatografie afinitní metody MeSH
- krystalografie rentgenová metody MeSH
- muramidasa * chemie genetika izolace a purifikace MeSH
- mutace * MeSH
- Publikační typ
- časopisecké články 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.
Citace poskytuje Crossref.org
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