Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Protein Science

ISSN

0961-8368

e-ISSN

—

Svazek periodika

26

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

1116-1123

Kód UT WoS článku

000403919400003

EID výsledku v databázi Scopus

2-s2.0-85017169069