Structure of mouse L-chain ferritin at 1.6 Å resolution

Granier, T.; Gallois, B.; Langlois d'Estaintot, B.; Dautant, A.; Chevalier, J.-M.; Mellado, J.-M.; Beaumont, C.; Santambrogio, P.; Arosio, P.; Precigoux, G.

doi:10.1107/S0907444901008897

Structure of mouse L-chain ferritin at 1.6 Å resolution

T. Granier, B. Gallois, B. Langlois d'Estaintot, A. Dautant, J.-M. Chevalier, J.-M. Mellado, C. Beaumont, P. Santambrogio, P. Arosio and G. Precigoux

Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 Å resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight-amino-acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature.

Keywords: L-chain ferritin.

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Structure of mouse L-chain ferritin at 1.6 Å resolution

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