5I14

Truncated and mutated T4 lysozyme

Summary for 5I14

• Entry DOI: 10.2210/pdb5i14/pdb
• Descriptor: mutated and truncated T4 lysozyme, NICKEL (II) ION (3 entities in total)
• Functional Keywords: t4 lysozyme, hydrolase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 2
• Total formula weight: 27551.76

Authors

Klima, M.,Boura, E. (deposition date: 2016-02-05, release date: 2016-02-17, Last modification date: 2024-01-10)

Primary citation

Boura, E.,Baumlova, A.,Chalupska, D.,Dubankova, A.,Klima, M.
Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography.
Protein Sci., 26:1116-1123, 2017

PubMed Abstract: 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.

PubMed: 28342173
DOI: 10.1002/pro.3162

Experimental method

X-RAY DIFFRACTION (1.745 Å)