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Literature summary for 3.4.21.B34 extracted from
- Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum (2001), J. Struct. Biol., 134, 83-87.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop vapour diffusion method, forms crystals of octahedral morphology under low-ionic-strength conditions. Crystals belong to space group C2 with unit cell dimensions, a = 307.5 A, b = 163.2 A, c =220.9 A, beta = 105.5° and diffract to 2.2 A resolution | Thermoplasma acidophilum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermoplasma acidophilum | P96086 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermoplasma acidophilum |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | in vivo the hexamers assemble further to form large icosahedral capsids of 14.6 MDa | Thermoplasma acidophilum |
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