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1.  Time-Resolved Serial Crystallography Captures High Resolution Intermediates of Photoactive Yellow Protein 
Science (New York, N.Y.)  2014;346(6214):1242-1246.
Serial femtosecond crystallography using ultrashort pulses from X-ray Free Electron Lasers (XFELs) offers the possibility to study light-triggered dynamics of biomolecules. Using microcrystals of the blue light photoreceptor, photoactive yellow protein, as a model system, we present high resolution, time-resolved difference electron density maps of excellent quality with strong features, which allow the determination of structures of reaction intermediates to 1.6 Å resolution. These results open the way to the study of reversible and non-reversible biological reactions on time scales as short as femtoseconds under conditions which maximize the extent of reaction initiation throughout the crystal.
doi:10.1126/science.1259357
PMCID: PMC4361027  PMID: 25477465
2.  Preface for Special Issue on Biology with X-ray Lasers 2 
Structural Dynamics  2015;2(4):041501.
doi:10.1063/1.4928768
PMCID: PMC4711608  PMID: 26798799
3.  Bayesian algorithms for recovering structure from single-particle diffraction snapshots of unknown orientation: a comparison 
X-ray free-electron lasers are being used to determine the three-dimensional structure of objects from random snapshots. The two apparently very different Bayesian algorithms capable of performing this at ultra-low signal are fundamentally the same.
The advent of X-ray free-electron lasers promises the possibility to determine the structure of individual particles such as microcrystallites, viruses and biomolecules from single-shot diffraction snapshots obtained before the particle is destroyed by the intense femtosecond pulse. This program requires the ability to determine the orientation of the particle giving rise to each snapshot at signal levels as low as ~10−2 photons per pixel. Two apparently different approaches have recently demonstrated this capability. Here we show they represent different implementations of the same fundamental approach, and identify the primary factors limiting their performance.
doi:10.1107/S0108767311019611
PMCID: PMC3171899  PMID: 21844653
X-ray scattering; single-particle structure determination

Results 1-3 (3)