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High-brightness femtosecond-to-attosecond pulses are indispensable for probing electron dynamics on their fundamental temporal scales. X-ray free-electron lasers (XFELs) at high repetition rates will facilitate high-statistics measurements…
Structure determination is a key application of XFELs and 4th generation synchrotron sources, particularly using the coherent and pulsed X-ray radiation from X-ray free-electron lasers (XFEL). Scientific interest focuses on understanding…
X-ray free-electron lasers (FELs) are promising tools for structural determination of macromolecules via coherent x-ray scattering. During ultrashort and ultraintense x-ray pulses with an atomic scale wavelength, samples are subject to…
Single-particle imaging experiments of biomolecules at x-ray free-electron lasers (XFELs) require processing of hundreds of thousands (or more) of images that contain very few x-rays. Each low-flux image of the diffraction pattern is…
We demonstrate the potential of X-ray free-electron lasers (XFEL) to advancethe understanding of complex plasma dynamics by allowing for the first time nanometer and femtosecond resolution at the same time in plasma diagnostics. Plasma…
The advent of isolated and intense sub-femtosecond X-ray pulses enables tracking of quantummechanical motion of electrons in molecules and solids. The combination of X-ray spectroscopy and diffraction imaging is a powerful approach to…
During the last five years, serial femtosecond crystallography using x-ray laser pulses has developed into a powerful technique for determining the atomic structures of protein molecules from micrometer and sub-micrometer sized crystals.…
The resolution of X-ray diffraction microscopy is limited by the maximum dose that can be delivered prior to sample damage. In the proposed Serial Crystallography method, the damage problem is addressed by distributing the total dose over…
We present a comprehensive analysis of coherence properties of the radiation from X-ray free electron laser (XFEL). We consider practically important case when XFEL is optimized for maximum gain. Such an optimization allows to reduce…
Diffraction-before-destruction imaging with single ultrashort X-ray pulses has the potential to visualise non-equilibrium processes, such as chemical reactions, at the nanoscale with sub-femtosecond resolution in the native environment…
We present a theoretical justification for a method of extracting of supplementary information for the phase retrieval procedure taken from diffraction of fs-pulses from X-ray Free Electron Laser facilities. The approach is based on…
The advent of accelerator-driven free-electron lasers (FEL) has opened new avenues for high-resolution structure determination via diffraction methods that go far beyond conventional x-ray crystallography methods. These techniques rely on…
The current state of the art in structural biology is led by NMR, X-ray crystallography and TEM investigations. These powerful tools however all rely on averaging over a large ensemble of molecules. Here, we present an alternative concept…
X-ray single particle imaging (SPI) has offered the potential to visualize structures of biomolecules at near-atomic resolution. However, state-of-the-art structures at X-ray free electron lasers (XFELs) are limited to moderate resolution,…
X-ray free-electron lasers (XFELs) of high brightness have opened new opportunities for exploring ultrafast dynamical processes in matter, enabling imaging and movies of single molecules and particles at atomic resolution. In this paper, we…
The European X-ray Free Electron Laser (XFEL) will deliver 30,000 fully coherent, high brilliance X-ray pulses per second each with a duration below 100 fs. This will allow the recording of diffraction patterns of single complex molecules…
X-ray free-electron lasers (FEL) deliver ultrabright X-ray pulses, but not the sequences of phase-coherent pulses required for time-domain interferometry and control of quantum states. For conventional split-and-delay schemes to produce…
The mode of action of proteins is to a large extent given by their ability to adopt different conformations. This is why imaging single biomolecules at atomic resolution is one of the ultimate goals of biophysics and structural biology. The…
The development of X-ray Free Electron Lasers (XFELs) has opened numerous opportunities to probe atomic structure and ultrafast dynamics of various materials. Single Particle Imaging (SPI) with XFELs enables the investigation of biological…
X-ray Free-Electron Lasers (XFELs) deliver X-ray pulses with a coherent flux that is approximately eight orders of magnitude greater than that available from a modern third generation synchrotron source. The power density in an XFEL pulse…