Native phasing of x-ray free-electron laser data for a G protein–coupled receptor

+ See all authors and affiliations

Science Advances  23 Sep 2016:
Vol. 2, no. 9, e1600292
DOI: 10.1126/sciadv.1600292

You are currently viewing the abstract.

View Full Text


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.

  • Crystallography
  • x-ray free electron laser
  • serial femtosecond crystallography
  • SAD
  • sulfur
  • GPCR
  • lipidic cubic phase
  • native phasing
  • de novo structure
  • protein

This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license, which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.

View Full Text

More Like This