title: Structure of mouse L-chain ferritin at 1.6 A resolution.
abstract: 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.
authors.affiliation: Unité de Biophysique Structurale, UMR CNRS 5471, Université Bordeaux I, Bâtiment B8, Avenue des Facultés, 33405 Talence CEDEX, France. t.granier@ubs.u-bordeaux.fr
authors.forename: T
authors.initials: T
authors.lastname: Granier
authors.forename: B
authors.initials: B
authors.lastname: Gallois
authors.forename: B
authors.initials: B
authors.lastname: Langlois d'Estaintot
authors.forename: A
authors.initials: A
authors.lastname: Dautant
authors.forename: J M
authors.initials: JM
authors.lastname: Chevalier
authors.forename: J M
authors.initials: JM
authors.lastname: Mellado
authors.forename: C
authors.initials: C
authors.lastname: Beaumont
authors.forename: P
authors.initials: P
authors.lastname: Santambrogio
authors.forename: P
authors.initials: P
authors.lastname: Arosio
authors.forename: G
authors.initials: G
authors.lastname: Precigoux
mesh_terms: D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D005293:Ferritins / Q000737:chemistry*; D006860:Hydrogen Bonding; D008670:Metals / Q000378:metabolism; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012492:Salts / Q000737:chemistry; D013696:Temperature
chemical_list: D008670:Metals; D011994:Recombinant Proteins; D012492:Salts; D005293:Ferritins