Structure of mouse L-chain ferritin at 1.6 angstrom resolution

Citation
T. Granier et al., Structure of mouse L-chain ferritin at 1.6 angstrom resolution, ACT CRYST D, 57, 2001, pp. 1491-1497
Citations number
29
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
11
Pages
1491 - 1497
Database
ISI
SICI code
0907-4449(200111)57:<1491:SOMLFA>2.0.ZU;2-F
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 Angstrom resolution from data obtained at room temperature and under cryogenic conditions, resp ectively. 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 l ow temperature.