The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure.

@article{Okada2004TheRC,
  title={The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure.},
  author={Tetsuji Okada and Minoru Sugihara and Ana-Nicoleta Bondar and Marcus Elstner and Peter Entel and Volker Buss},
  journal={Journal of molecular biology},
  year={2004},
  volume={342 2},
  pages={571-83}
}
A new high-resolution structure is reported for bovine rhodopsin, the visual pigment in rod photoreceptor cells. Substantial improvement of the resolution limit to 2.2 A has been achieved by new crystallization conditions, which also reduce significantly the probability of merohedral twinning in the crystals. The new structure completely resolves the polypeptide chain and provides further details of the chromophore binding site including the configuration about the C6-C7 single bond of the 11… CONTINUE READING
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