Crystallization (Comment) | Organism |
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the crystal structure of the switch mutant L20/R63A liganded to both methyl- and ethylguanidinium ions is determined at resolutions of 1.7 A and 1.8 A, respectively | Tequatrovirus T4 |
Protein Variants | Comment | Organism |
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additional information | L20 is a mutant with a molecular switch in a T4 lysozyme construct that promotes a large-scale (about 20 A) translocation of an alpha-helix but is unrelated to the function of the protein. The design is based in part on the use of a duplicated helical sequenc. When Arg63 is truncated to Ala (in mutant L20/R63A), the stability of the protein is reduced by 6.1°C relative to L20. In high salt buffer similar to that used for crystallization, the melting temperature of L20/R63A is increased by 2.2°C in the presence of either 200 mM methylguanidinium or 200 mM ethylguanidinium ion | Tequatrovirus T4 |
Organism | UniProt | Comment | Textmining |
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Tequatrovirus T4 | P00720 | - |
- |