Structure of mouse L-chain ferritin at 1.6 A resolution.
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.
Granier
T
T
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
Gallois
B
B
Langlois d'Estaintot
B
B
Dautant
A
A
Chevalier
J M
JM
Mellado
J M
JM
Beaumont
C
C
Santambrogio
P
P
Arosio
P
P
Precigoux
G
G
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
D008670:Metals; D011994:Recombinant Proteins; D012492:Salts; D005293:Ferritins