Serial femtosecond crystallography of soluble proteins in lipidic cubic phase

By Raimund Fromme, Andrii Ishchenko, Markus Metz, Shatabdi Roy Chowdhury1, Shibom Basu1, Sébastien Boutet, Petra Fromme1, Thomas A. White, Anton Barty, John Spence1, Uwe Weierstall1, Wei Liu1, Vadim Cherezov2

1. Arizona State University 2. Bridge Institute - University of Southern California

See also

No results found.

Published on





Raimund Fromme and Andrii Ishchenko and Markus Metz and Shatabdi Roy Chowdhury and Shibom Basu and Sébastien Boutet and Petra Fromme and Thomas A. White and Anton Barty and John C. H. Spence and Uwe Weierstall and Wei Liu and Vadim Cherezov


Fromme, R. et al., 2015. Serial femtosecond crystallography of soluble proteins in lipidic cubic phase. IUCrJ, 2(5), pp.545–551. Available at:


Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) enables high-resolution protein structure determination using micrometre-sized crystals at room temperature with minimal effects from radiation damage. SFX requires a steady supply of microcrystals intersecting the XFEL beam at random orientations. An LCP–SFX method has recently been introduced in which microcrystals of membrane proteins are grown and delivered for SFX data collection inside a gel-like membrane-mimetic matrix, known as lipidic cubic phase (LCP), using a special LCP microextrusion injector. Here, it is demonstrated that LCP can also be used as a suitable carrier medium for microcrystals of soluble proteins, enabling a dramatic reduction in the amount of crystallized protein required for data collection compared with crystals delivered by liquid injectors. High-quality LCP–SFX data sets were collected for two soluble proteins, lysozyme and phycocyanin, using less than 0.1 mg of each protein.




NSF-STC Biology with X-ray Lasers (NSF-1231306)