Surface of bacteriorhodopsin revealed by high-resolution electron crystallography

@article{Kimura1997SurfaceOB,
  title={Surface of bacteriorhodopsin revealed by high-resolution electron crystallography},
  author={Yoshiaki Kimura and Dmitry G. Vassylyev and Atsuo Miyazawa and Akinori Kidera and Masaaki Matsushima and Kaoru Mitsuoka and Kazuyoshi Murata and Teruhisa Hirai and Yoshinori Fujiyoshi},
  journal={Nature},
  year={1997},
  volume={389},
  pages={206-211}
}
Bacteriorhodopsin is a transmembrane protein that uses light energy, absorbed by its chromophore retinal, to pump protons from the cytoplasm of bacteria such as Halobacterium salinarium into the extracellular space,. It is made up of seven α-helices, and in the bacterium forms natural, two-dimensional crystals called purple membranes. We have analysed these crystals by electron cryo-microscopy to obtain images of bacteriorhodopsin at 3.0 å resolution. The structure covers nearly all 248 amino… CONTINUE READING

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