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Structure of mouse L-chain ferritin at 1.6 A resolution
T Granier1, B Gallois, B Langlois d'Estaintot
1Unité de Biophysique Structurale, UMR CNRS 5471, Université Bordeaux I, Bâtiment B8, Avenue des Facultés, 33405 Talence CEDEX, France. t.granier@ubs.u-bordeaux.fr
Acta Crystallographica. Section D, Biological Crystallography
|October 27, 2001
Summary
Cubic crystals of mouse L-chain apoferritin were analyzed. An eight-amino-acid loop insertion in the mouse sequence showed high disorder, regardless of temperature conditions.
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Apoferritin is a protein that stores iron.
- Understanding protein structure is crucial for function.
- Recombinant proteins allow for structural studies.
Purpose of the Study:
- To determine the crystal structure of recombinant mouse L-chain apoferritin.
- To investigate the structural impact of an eight-amino-acid loop insertion.
Main Methods:
- Crystallization using the hanging-drop technique with ammonium sulfate and cadmium sulfate.
- X-ray diffraction data collection at room temperature and cryogenic conditions.
- Structure refinement to 2.1 Å and 1.6 Å resolution.
Main Results:
- Successfully obtained cubic F432 crystals of mouse L-chain apoferritin.
- Refined the protein structure to high resolution.
- Identified significant disorder in an eight-amino-acid loop insertion across different temperatures.
Conclusions:
- The crystal structure of mouse L-chain apoferritin was elucidated.
- The eight-amino-acid loop insertion exhibits inherent structural flexibility or disorder.
- This finding has implications for understanding apoferritin function and dynamics.
