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High Pressure Single Crystal Diffraction at PX^2
Published on: January 16, 2017
Feasibility of one-shot-per-crystal structure determination using Laue diffraction.
Sterling Cornaby1, Doletha M E Szebenyi, Detlef-M Smilgies
1School of Applied and Engineering Physics, Cornell University, Ithaca, New York, USA.
Acta Crystallographica. Section D, Biological Crystallography
|January 9, 2010
Summary
Using single Laue images from multiple protein crystals can determine structures. This polychromatic Laue technique is effective even with limited data from small crystals, overcoming radiation damage limitations.
Area of Science:
- Structural biology
- Crystallography
- Biophysics
Background:
- Crystal size impacts data collection due to radiation damage.
- Small crystals yield limited diffraction patterns, necessitating multi-crystal datasets.
- Monochromatic methods face challenges with single-crystal exposures.
Purpose of the Study:
- To evaluate the feasibility of structure determination using single Laue images from multiple protein crystals.
- To assess the effectiveness of the polychromatic Laue technique for small crystals.
Main Methods:
- Data collection using a 'pink' beam at CHESS D1 station.
- Utilized lysozyme crystals (20-30 micrometers) mounted on MicroMesh grids.
- Employed single-shot Laue data for structure determination.
Main Results:
- Successful structure determination via molecular replacement using single Laue images.
- Obtained correct solutions even with data from as few as five crystals.
- Demonstrated the viability of the polychromatic Laue technique for small crystals.
Conclusions:
- Single Laue images from multiple small protein crystals are sufficient for structure determination.
- The polychromatic Laue technique offers a viable alternative to monochromatic methods for limited crystal samples.
- This approach mitigates issues associated with crystal size and radiation damage in structural biology.
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