High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography
SLAC National Accelerator Laboratory · Linac Coherent Light Source · +14 more institutions
Abstract
Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.
Citation impact
- FWCI
- 44.39
- Percentile
- 100%
- References
- 26
Authors
54- SBSébastien BoutetCorresponding
SLAC National Accelerator Laboratory, Linac Coherent Light Source
- LLLukas Lomb
Universität Hamburg, Max Planck Institute for Medical Research, Center for Free-Electron Laser Science
- GJGarth J. Williams
SLAC National Accelerator Laboratory, Linac Coherent Light Source
- TRThomas R. M. Barends
Universität Hamburg, Max Planck Institute for Medical Research, Center for Free-Electron Laser Science
- AAAndrew Aquila
Universität Hamburg, Deutsches Elektronen-Synchrotron DESY, Center for Free-Electron Laser Science
Topics & keywords
- Femtosecond
- Protein crystallization
- Crystallography
- Resolution (logic)
- Micrometer
- Diffraction
- X-ray crystallography
- Synchrotron