The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore.

@article{Wilmann2005The2C,
  title={The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore.},
  author={Pascal G. Wilmann and Jan Phillip Petersen and Anne Pettikiriarachchi and Ashley M. Buckle and Sean C. Smith and Seth Olsen and Matthew A. Perugini and Rodney J Devenish and Mark Prescott and Jamie Rossjohn},
  journal={Journal of molecular biology},
  year={2005},
  volume={349 1},
  pages={223-37}
}
We have determined the crystal structure of HcRed, a far-red fluorescent protein isolated from Heteractis crispa, to 2.1A resolution. HcRed was observed to form a dimer, in contrast to the monomeric form of green fluorescent protein (GFP) or the tetrameric forms of the GFP-like proteins (eqFP611, Rtms5 and DsRed). Unlike the well-defined chromophore conformation observed in GFP and the GFP-like proteins, the HcRed chromophore was observed to be considerably mobile. Within the HcRed structure… CONTINUE READING

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