Literature summary extracted from
Bosch, J.; Tamura, T.; Bourenkov, G.; Baumeister, W.; Essen, L.O.
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)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.21.B34 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.B34 |
Thermoplasma acidophilum |
P96086 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.21.B34 |
- |
Thermoplasma acidophilum |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.21.B34 |
hexamer |
in vivo the hexamers assemble further to form large icosahedral capsids of 14.6 MDa |
Thermoplasma acidophilum |