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Membrane protein structural biology using X-ray free electron lasers.
Richard Neutze1, Gisela Brändén1, Gebhard F X Schertler2
1Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, 40530 Gothenburg, Sweden.
Current Opinion in Structural Biology
|September 7, 2015
Summary
X-ray free electron lasers (XFELs) offer unprecedented brilliance for membrane protein structural biology, enabling damage-free structures. Choosing between synchrotron and XFEL radiation will advance understanding of membrane protein structure and dynamics.
Area of Science:
- Structural biology
- Biophysics
- Biochemistry
Background:
- Membrane protein structural biology heavily relies on synchrotron radiation sources for micro-focus crystallography.
- X-ray free electron lasers (XFELs) provide a significant increase in X-ray brilliance, offering a disruptive technology for the field.
Purpose of the Study:
- To explore the impact and potential of X-ray free electron lasers (XFELs) in membrane protein structural biology.
- To compare the utility of synchrotron radiation and XFELs for determining membrane protein structures and dynamics.
Main Methods:
- Serial femtosecond crystallography (SFX) using XFELs.
- XFEL-based structural studies on membrane proteins and 2D arrays.
- Time-resolved studies including SFX, wide-angle X-ray scattering, and X-ray emission spectroscopy.
Main Results:
- XFELs have been successfully used for proof-of-principle studies in membrane protein crystallography.
- XFEL data can yield crystallographic structures with minimal radiation damage.
- Serial crystallography methods, initially developed for XFELs, are now being applied to synchrotron radiation.
Conclusions:
- XFELs represent a transformative technology for membrane protein structural biology.
- A strategic selection between synchrotron and XFEL radiation sources will expedite discoveries in membrane protein structure and dynamics.
