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Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
Published on: September 20, 2016
High-resolution protein structure determination by serial femtosecond crystallography
Sébastien Boutet1, Lukas Lomb, Garth J Williams
1Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA. sboutet@slac.stanford.edu
Science (New York, N.Y.)
|June 2, 2012
Summary
Serial femtosecond crystallography (SFX) with an X-ray free-electron laser (XFEL) successfully determined high-resolution protein structures from microcrystals. This breakthrough offers a new method for analyzing difficult-to-crystallize molecules.
Area of Science:
- Structural biology
- Biophysics
- Crystallography
Background:
- Macromolecular structure determination traditionally relies on large, high-quality crystals.
- Radiation damage and crystal size limitations hinder analysis of many important biomolecules.
Purpose of the Study:
- To demonstrate the utility of serial femtosecond crystallography (SFX) for high-resolution structure determination.
- To analyze microcrystals of a model protein using X-ray free-electron laser (XFEL) technology.
Main Methods:
- Application of serial femtosecond crystallography (SFX).
- Utilizing an X-ray free-electron laser (XFEL) source.
- Analysis of microcrystals (sub-micrometer dimensions) of the protein lysozyme.
Main Results:
- High-resolution structural information was obtained from microcrystals.
- The results from SFX showed excellent agreement with synchrotron data.
- Demonstrated feasibility of SFX for challenging samples.
Conclusions:
- SFX is a viable and powerful technique for macromolecular structure determination.
- This method expands the scope of structural analysis to include difficult-to-crystallize proteins.
- Immediate relevance for studying a wide range of biomolecules previously inaccessible to structural analysis.
