Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00477107" target="_blank" >RIV/61388963:_____/17:00477107 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/pro.3162" target="_blank" >http://dx.doi.org/10.1002/pro.3162</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/pro.3162" target="_blank" >10.1002/pro.3162</a>
Alternative languages
Result language
angličtina
Original language name
Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein Science
ISSN
0961-8368
e-ISSN
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Volume of the periodical
26
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
1116-1123
UT code for WoS article
000403919400003
EID of the result in the Scopus database
2-s2.0-85017169069