Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution.

  title={Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution.},
  author={Stephen K. Ritter and Roger G. Hiller and P M Wrench and Wolfram Welte and Kay Diederichs},
  journal={Journal of structural biology},
  volume={126 2},
The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-A resolution by molecular replacement, using the atomic coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model. The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer with an internal noncrystallographic dyad and a fragment of the gamma-polypeptide. The alpha-polypeptide… CONTINUE READING


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