Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.

@article{Lwe1995CrystalSO,
  title={Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.},
  author={J. L{\"o}we and D. Stock and B. Jap and P. Zwickl and W. Baumeister and R. Huber},
  journal={Science},
  year={1995},
  volume={268 5210},
  pages={
          533-9
        }
}
The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta… Expand
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