Free-electron lasers reveal detailed architecture of proteins
(Phys.org) -- In the centennial year of Max von Laues discovery that X-ray diffraction can be used to unravel the atomic architecture of molecules, a new approach to the determination of high-resolution structures has been demonstrated. An international team of researchers has analyzed tiny protein crystals using short pulses of X-ray light from the worlds first hard X-ray free-electron laser, the US Department of Energys 300 million dollar Linac Coherent Light Source at Stanford. The study demonstrates the immense potential of free-electron lasers for obtaining the structures of macromolecules from tiny crystals when illuminated with the blazing intensity of the ultrashort free-electron laser X-ray pulses, even though the crystals are destroyed in the process. In the current study, their structural analysis reveals details with a spatial resolution of 0.2 millionth of a millimeter.