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Global radiation damage: temperature dependence, time dependence and how to outrun it
Matthew Warkentin1, Jesse B Hopkins, Ryan Badeau
1Physics Department, Cornell University, Ithaca, NY 14853, USA.
Global radiation damage to protein crystals above 200 K is limited by solvent diffusion. Faster data collection at higher doses can minimize damage, enabling more native protein studies.
Area of Science:
- Crystallography
- Structural Biology
- Radiation Physics
Background:
- Protein crystals are susceptible to radiation damage during X-ray diffraction.
- Understanding radiation damage mechanisms is crucial for accurate structural determination.
Purpose of the Study:
- To elucidate the mechanisms of global radiation damage in protein crystals.
- To identify strategies for minimizing radiation damage at various temperatures.
Main Methods:
- Analysis of radiation damage effects across a range of temperatures (above ~200 K).
- Investigation of damage timescales and their dependence on temperature.
- Correlation of damage with solvent-coupled diffusive processes.
Main Results:
- A distinct transition in radiation sensitivity occurs near 200 K.
- Above 200 K, damage is primarily governed by solvent-coupled diffusion.
- Damage timescales decrease from minutes at 180 K to seconds near room temperature.
- Rapid data collection (1s) can outrun significant damage at 260 K.
Conclusions:
- Radiation damage mechanisms in protein crystals are temperature-dependent.
- Minimizing radiation damage is achievable by optimizing data collection strategies.
- Higher dose rates with microfocused beams offer potential for near-native structural studies.
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