Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A 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.
Structure of mouse L-chain ferritin at 1.6 A resolution.,Granier T, Gallois B, Langlois d'Estaintot B, Dautant A, Chevalier JM, Mellado JM, Beaumont C, Santambrogio P, Arosio P, Precigoux G Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1491-7. Epub 2001, Oct 25. PMID:11679711[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Granier T, Gallois B, Langlois d'Estaintot B, Dautant A, Chevalier JM, Mellado JM, Beaumont C, Santambrogio P, Arosio P, Precigoux G. Structure of mouse L-chain ferritin at 1.6 A resolution. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1491-7. Epub 2001, Oct 25. PMID:11679711
