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On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
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Pink-beam serial crystallography
A Meents1,2, M O Wiedorn3,4, V Srajer5
1Center for Free Electron Laser Science, DESY, Notkestrasse 85, 22607, Hamburg, Germany. alke.meents@desy.de.
Nature Communications
|November 4, 2017
Summary
Researchers used pink-beam X-ray pulses to determine protein structures faster than ever before. This new method enables studying rapid biological processes at sub-microsecond timescales.
Area of Science:
- Structural Biology
- Biophysics
- X-ray Science
Background:
- Serial X-ray crystallography enables macromolecular structure determination at X-ray free electron lasers (XFELs) and synchrotron sources.
- Current time resolution for serial synchrotron crystallography is limited to millisecond timescales using monochromatic beams.
Purpose of the Study:
- To investigate the potential of polychromatic (pink) X-ray beams for time-resolved diffraction experiments at synchrotron sources.
- To achieve significantly shorter timescales than previously possible with monochromatic beams.
Main Methods:
- Utilized a pink-beam setup with a highly focused, high-photon-flux X-ray pulse (100 ps exposure) per crystal.
- Optimized the experimental setup for very low scattering background.
- Merged diffraction patterns from numerous small crystals to obtain complete datasets.
Main Results:
- Successfully determined the structures of two different protein samples.
- Required data from only 50 crystals, a significant reduction compared to monochromatic experiments.
- Achieved high-quality diffraction data, demonstrating the method's efficacy.
Conclusions:
- Pink-beam serial synchrotron crystallography enables structure determination at sub-microsecond timescales.
- This technique significantly enhances the study of rapid, irreversible biological reactions.
- High-brightness X-ray facilities can be leveraged for unprecedented time-resolved structural studies.

