Crystallization (Comment) | Organism |
---|---|
purified enzyme, hanging drop vapour diffusion method, 0.001 ml of 8 mg/ml protein in 150 mM NaCl and 50 mM HEPES, pH 7.25, is mixed with 0.001 ml of reservoir solutions containing 43-45% ammonium sulfate, 0.01 M cobalt chloride, and 0.1 M MES, pH 6.25-6.5, 22°C, 3 weeks, X-ray diffraction structure determination and analysis at 1.75 A resolution | Salmo salar |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Salmo salar | A6PZ97 | - |
- |
Renatured (Comment) | Organism |
---|---|
unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Refolding is dramatically reduced in solutions with high SalG concentrations, coupled with significant protein precipitation. Rapid and irreversible inactivation takes place during heating at high enzyme concentration | Salmo salar |
Subunits | Comment | Organism |
---|---|---|
More | structure homology modeling, overview | Salmo salar |
Synonyms | Comment | Organism |
---|---|---|
Goose-type lysozyme | - |
Salmo salar |
SalG | - |
Salmo salar |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Rapid and irreversible inactivation takes place during heating at high enzyme concentration | Salmo salar |