Structural description of the active sites of mouse L-chain ferritin at 1.2 Å resolution

@article{Granier2002StructuralDO,
  title={Structural description of the active sites of mouse L-chain ferritin at 1.2 {\AA} resolution},
  author={Thierry Granier and B{\'e}atrice Langlois d'Estaintot and Bernard M. Gallois and Jean Marc Chevalier and Gilles Pr{\'e}cigoux and Paolo Santambrogio and Paolo Arosio},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2002},
  volume={8},
  pages={105-111}
}
Abstract. The first ferritin structure refined at the atomic level has been achieved on recombinant mouse L-chain apoferritin (rMoLF) crystals. These latter diffract to 1.2 Å resolution under cryogenic conditions. When cryo-cooling the sample, the thermal disorder usually observed at room temperature is reduced and the low-temperature structure reveals several details concerning the protein putative active sites and their properties. Within the pores built up by the molecular three-fold… 
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Results indicate that the C-terminal regions have an important role in the activity of the ferroxidase center and the stability of rCtFtn.
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References

SHOWING 1-2 OF 2 REFERENCES
Protein Express Purif
  • 2000
SHELXL97. University of Göttingen, Germany
  • 1997