EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.26.4 | purified recombinant wild-type enzyme, X-ray diffraction structure determination and analysis at 1.66-1.72 A resolution | Sulfurisphaera tokodaii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.26.4 | C58A/C145A | site-directed mutagenesis | Sulfurisphaera tokodaii |
3.1.26.4 | additional information | the Sto-RNase HI C-terminal residues, -IGCIILT, are introduced as a tag on three proteins. Each chimeric protein is more stable than its wild-type protein | Sulfurisphaera tokodaii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.26.4 | Sulfurisphaera tokodaii | - |
- |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.26.4 | RNase HI | - |
Sulfurisphaera tokodaii |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.26.4 | additional information | - |
the C-terminal of RNase HI from the hyperthermophile Sulfolobus tokodaii does not affect overall structure, and thermal stabilization is caused by local interactions of the C-terminal, suggesting that the C-terminal residues could be used as a stabilization tag. Thermodynamic measurements of the stability of variants lacking the disulfide bond, C58/145A, or the six C-terminal residues (DELTAC6) and by structural analysis of DELTAC6, overview | Sulfurisphaera tokodaii |