Abstract

Electron microscopy and X-ray crystallography provide unique insight into the architecture of cells, molecular assemblies and (macro)molecules. Ultimately, both methods are limited by radiation damage. Compared to synchrotron sources, free-electron lasers (FEL) provide orders of magnitude brighter and shorter X-ray pulses that have been proposed to yield diffraction patterns of biological samples before the onset of significant radiation damage (“diffraction before destruction”). Recently, the Linac Coherent Light Source (LCLS) has become accessible to users, accessing the hard X-ray regime, thereby allowing Angstrom-resolution studies with femtosecond time resolution. This enables a plethora of new experiments, including femtochemistry and the structural analysis of complex materials, warm dense matter, and biological samples. The latter include single particles such as viruses. Recent results will be described that were obtained by a collaboration consisting of the Max Planck Advanced Study Group at CFEL, CFEL DESY, Arizona State University, SLAC, Uppsala University, LLNL, and University of Wisconsin-Milwaukee. The LCLS is operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences.

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