Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

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.
    View publication on PubMed

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