In:
Science Advances, American Association for the Advancement of Science (AAAS), Vol. 2, No. 9 ( 2016-09-02)
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 A 2A 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.
Type of Medium:
Online Resource
ISSN:
2375-2548
DOI:
10.1126/sciadv.1600292
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2016
detail.hit.zdb_id:
2810933-8