Molecular Imaging Using X-Ray Free-Electron Lasers

X-ray crystallography, which is used for the determination of most biomolecular structures, has relied on Bragg diffraction from single crystals for more than a century. For many difficult to crystallize proteins, the growth of large well-ordered single crystals is a major challenge. Single molecule diffraction is a challenging but highly desired approach to structure determination, as it abolishes the need for crystallization and provides about four times higher information content than needed to solve a structure, unlike Bragg diffraction which is usually insufficient for direct phasing. Even using the powerful X-ray Free Electron Lasers, the challenges of this method have so far not been overcome to acquire atomic resolution structures. Recently, it was shown that the structure of a protein can be solved based on continuous diffraction from crystals with translational disorder.