Native phasing of x-ray free-electron laser data for a G protein-coupled receptor
Category
Published on
Type
journal-article
Author
Alexander Batyuk and Lorenzo Galli and Andrii Ishchenko and Gye Won Han and Cornelius Gati and Petr A. Popov and Ming-Yue Lee and Benjamin Stauch and Thomas A. White and Anton Barty and Andrew Aquila and Mark S. Hunter and Mengning Liang and Sébastien Boutet and Mengchen Pu and Zhi-jie Liu and Garrett Nelson and Daniel James and Chufeng Li and Yun Zhao and John C. H. Spence and Wei Liu and Petra Fromme and Vsevolod Katritch and Uwe Weierstall and Raymond C. Stevens and Vadim Cherezov
Citation
Batyuk, A. et al., 2016. Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Science Advances, 2(9), pp.e1600292–e1600292. Available at: http://dx.doi.org/10.1126/sciadv.1600292.
Abstract
Serial femtosecond crystallography (SFX) takes advantage of extremely bright and ultrashort pulses produced by x-ray free-electron lasers (XFELs), allowing for the collection of high-resolution diffraction intensities from micrometer-sized crystals at room temperature with minimal radiation damage, using the principle of “diffraction-before-destruction.” However, de novo structure factor phase determination using XFELs has been difficult so far. We demonstrate the ability to solve the crystallographic phase problem for SFX data collected with an XFEL using the anomalous signal from native sulfur atoms, leading to a bias-free room temperature structure of the human A2A adenosine receptor at 1.9 Å resolution. The advancement was made possible by recent improvements in SFX data analysis and the design of injectors and delivery media for streaming hydrated microcrystals. This general method should accelerate structural studies of novel difficult-to-crystallize macromolecules and their complexes.
DOI
Funding
NSF-STC Biology with X-ray Lasers (NSF-1231306)
