A crystallographic study of bright far-red fluorescent protein mKate reveals pH-induced cis-trans isomerization of the chromophore.

@article{Pletnev2008ACS,
  title={A crystallographic study of bright far-red fluorescent protein mKate reveals pH-induced cis-trans isomerization of the chromophore.},
  author={Sergei Pletnev and Dmitry S. Shcherbo and Dmitriy M Chudakov and Nadezhda V Pletneva and Ekaterina M. Merzlyak and Alexander Wlodawer and Zbigniew Dauter and Vladimir Pletnev},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 43},
  pages={28980-7}
}
The far-red fluorescent protein mKate (lambda(ex), 588 nm; lambda(em), 635 nm; chromophore-forming triad Met(63)-Tyr(64)-Gly(65)), originating from wild-type red fluorescent progenitor eqFP578 (sea anemone Entacmaea quadricolor), is monomeric and characterized by the pronounced pH dependence of fluorescence, relatively high brightness, and high photostability. The protein has been crystallized at a pH ranging from 2 to 9 in three space groups, and four structures have been determined by x-ray… CONTINUE READING
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