Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase

@article{Chan1995StructureOA,
  title={Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase},
  author={Mk Chan and Swarnalatha Mukund and Arnulf Kletzin and M. W. W. Adams and D. C. Rees},
  journal={Science},
  year={1995},
  volume={267},
  pages={1463 - 1469}
}
The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe4S4 cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum… 

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