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Literature summary for 1.6.2.2 extracted from
- Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution (2007), Acta Crystallogr. Sect. F, F63, 274-279.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapour-diffusion method | Physarum polycephalum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Physarum polycephalum | - |
expressed in Escherichia coli | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cyt b5R protein | - |
Physarum polycephalum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 51 | - |
denaturation temperature. The difference in the hydrophobic interactions in the Physarum polycephalum and human cyt b5R proteins is the primary factor underlying the lower denaturation temperature of Physarum polycephalum cyt b5R | Physarum polycephalum |
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