High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography
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.
Image: (A) The electron density map; (B) the difference Fourier map.
Boutet, S., Lomb, L., Williams, G.J., Barends, T.R.M., Aquila, A., Doak, R.B., Weierstall, U., DePonte, D.P., Steinbrener, J., Shoeman, R.L. & (2012). High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography, Science, 337 (6092) 364. DOI: 10.1126/science.1217737