X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolution.

@article{Serre1996XraySO,
  title={X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolution.},
  author={Laurence Serre and Fr{\'e}d{\'e}ric M. D. Vellieux and Milagros Medina and Carlos G{\'o}mez-Moreno and Juan C Fontecilla-Camps and Monika Frey},
  journal={Journal of molecular biology},
  year={1996},
  volume={263 1},
  pages={20-39}
}
The crystal structure of the ferredoxin:NADP+ reductase (FNR) from the cyanobacterium Anabaena PCC 7119 has been determined at 2.6 A resolution by multiple isomorphous replacement and refined using 15.0 A to 1.8 A data, collected at 4 degrees C, to an R-factor of 0.172. The model includes 303 residues, the flavin adenine dinucleotide cofactor (FAD), one sulfate ion located at the putative NADP+ binding site and 328 water molecule sites. The structure of Anabaena FNR, including FAD, a network of… CONTINUE READING
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