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Radiation driven collapse of protein crystals
Sébastien Boutet1, Ian K Robinson
1Department of Physics, University of Illinois, Urbana, IL 61801, USA.
Journal of Synchrotron Radiation
|December 24, 2005
Summary
Ferritin crystals underwent a sudden lattice contraction and collapse during X-ray diffraction experiments. Analysis revealed 55% of layers contracted by 1.6% before diffraction ceased.
Area of Science:
- Materials Science
- Crystallography
- Biophysics
Background:
- Ferritin is a protein crucial for iron storage in cells.
- Understanding ferritin's structural dynamics under external stimuli is important.
- Coherent X-ray diffraction is a powerful tool for studying crystal structures.
Purpose of the Study:
- To investigate the structural response of ferritin crystals to X-ray radiation.
- To analyze the mechanism and progression of crystal lattice collapse.
- To apply a theoretical model to describe the observed phenomenon.
Main Methods:
- Coherent X-ray diffraction measurements were performed on ferritin crystals.
- Experiments were conducted at room temperature using monochromatic undulator radiation.
- Data analysis involved a two-state Hendricks-Teller model.
Main Results:
- A sudden lattice contraction was observed in ferritin crystals.
- A characteristic latent period preceded the crystal collapse.
- The Hendricks-Teller model indicated 55% of layers collapsed by 1.6% before diffraction ceased.
Conclusions:
- Ferritin crystals exhibit a distinct collapse behavior under X-ray irradiation.
- The observed phenomenon can be modeled using the Hendricks-Teller approach.
- This study provides insights into the mechanical stability and X-ray sensitivity of ferritin.