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Literature summary for 2.5.1.78 extracted from
- X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons (2001), J. Mol. Biol., 306, 1099-1114.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Aquifex aeolicus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallized at room temperature by sitting-drop vapor-diffusion method, the protein is crystallized in the cubic space group I23 with the cell dimensions a = b = c = 180.8 A, diffraction data are collected to 1.6 A resolution | Aquifex aeolicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aquifex aeolicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Aquifex aeolicus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 60-mer | the spherical protein consists of 60 identical subunits with strict icosahedral 532 symmetry | Aquifex aeolicus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 120 | - |
melting temperature: 119.9°C | Aquifex aeolicus |
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Release 2023.1 (January 2023)
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