Journal
SCIENCE ADVANCES
Volume 2, Issue 9, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.1600292
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Funding
- NIH [R01 GM108635, U54 GM094618, U54 GM094599, R01 GM095583, P41 GM103393, P41 RR001209]
- Ministry of Science and Technology of China [2014CB910400]
- NSF Science and Technology Center [1231306]
- Russian Ministry of Education and Science [5-100]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
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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 angstrom 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.
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