The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.

@article{Bode1988The2A,
  title={The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.},
  author={Wolfram Bode and Richard Alan Engh and Danette Musil and Uwe Thiele and Robert Huber and A Karshikov and Jo{\vz}e Brzin and Janko Kos and Vito Turk},
  journal={The EMBO journal},
  year={1988},
  volume={7 8},
  pages={2593-9}
}
The crystal structure of chicken egg white cystatin has been solved by X-ray diffraction methods using the multiple isomorphous replacement technique. Its structure has been refined to a crystallographic R value of 0.19 using X-ray data between 6 and 2.0A. The molecule consists mainly of a straight five-turn alpha-helix, a five-stranded antiparallel beta-pleated sheet which is twisted and wrapped around the alpha-helix and an appending segment of partially alpha-helical geometry. The 'highly… CONTINUE READING
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