Abstract
Imaging biological macromolecules allows scientists to accurately probe dynamic molecular structures and engineer drugs. Brief and intense coherent x-ray pulses can yield new forms of data, enabling structure determination without prior-known structural information.
Highlights
Serial femtosecond crystallography (SFX) [1,2,3] exploits coherent, femtosecond-duration hard x-ray pulses produced by an x-ray free-electron laser (XFEL) to record diffraction patterns from protein crystals on a time scale that is faster than atomic motion [4]
Recent experimental work has indicated the need to merge tens or hundreds of thousands of XFEL diffraction patterns in order to observe intensities between proteincrystal Bragg reflections at moderate resolutions [24]; the low signal detected in individual patterns from protein crystals continues to be the primary challenge to directly applying iterative phasing on a pattern-by-pattern basis
We have demonstrated that this method for decoupling the average crystal-lattice transform from the underlying unit-cell transform is effective when the phase and intensity of the illuminating wavefront is noticeably nonuniform and varies from one crystal to the
Summary
Serial femtosecond crystallography (SFX) [1,2,3] exploits coherent, femtosecond-duration hard x-ray pulses produced by an x-ray free-electron laser (XFEL) to record diffraction patterns from protein crystals on a time scale that is faster than atomic motion [4]. Recent experimental work has indicated the need to merge tens or hundreds of thousands of XFEL diffraction patterns in order to observe intensities between proteincrystal Bragg reflections at moderate resolutions [24]; the low signal detected in individual patterns from protein crystals continues to be the primary challenge to directly applying iterative phasing on a pattern-by-pattern basis. Radiation damage makes this approach challenging at synchrotron sources [36]. The paper concludes with an analysis of the recovered structures and a discussion of the results
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