Structure of mouse L-chain ferritin at 1.6 A resolution

Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1491-7. doi: 10.1107/s0907444901008897. Epub 2001 Oct 25.

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.

MeSH terms

  • Animals
  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Ferritins / chemistry*
  • Hydrogen Bonding
  • Metals / metabolism
  • Mice
  • Models, Molecular
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Salts / chemistry
  • Temperature

Substances

  • Metals
  • Recombinant Proteins
  • Salts
  • Ferritins

Associated data

  • PDB/1AEW
  • PDB/1BG7
  • PDB/1DAT
  • PDB/1H96
  • PDB/1RCD
  • PDB/2FHA