Related papers: Structure determination from single-molecule X-ray…
Single molecule X-ray scattering experiments using free electron lasers hold the potential to resolve both single structures and structural ensembles of biomolecules. However, molecular electron density determination has so far not been…
Single molecule X-ray scattering experiments with free electron lasers have opened a new route to the structure determination of biomolecules. Because typically only very few photons per scattering image are recorded and thus the…
Femtosecond x-ray nanocrystallography exploiting XFEL radiation is an emerging method for protein structure determination using crystals with sizes ranging from a few tens to a few hundreds nanometers. Crystals are randomly hit by XFEL…
Resonant inelastic x-ray scattering (RIXS) is a widely used spectroscopic technique, providing access to the electronic structure and dynamics of atoms, molecules, and solids. However, RIXS requires a narrow bandwidth x-ray probe to achieve…
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…
Resonant inelastic x-ray scattering (RIXS) is a well-established tool for studying electronic, nuclear and collective dynamics of excited atoms, molecules and solids. An extension of this powerful method to a time-resolved probe technique…
The advent of X-ray Free Electron Lasers promises the possibility to determine the structure of individual particles such as microcrystallites, viruses and biomolecules from single-shot diffraction snapshots obtained before the particle is…
Single particle diffraction imaging experiments at free-electron lasers (FEL) have a great potential for structure determination of reproducible biological specimens that can not be crystallized. One of the challenges in processing the data…
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,…
Proposals to determine biomolecular structures from diffraction experiments using femtosecond X-ray free-electron laser (XFEL) pulses involve a conflict between the incident brightness required to achieve diffraction-limited atomic…
X-ray Free Electron Lasers (XFEL) are the most advanced pulsed x-ray sources. Their extraordinary pulse parameters promise unique applications. Indeed, several new methods have been developed at XFEL-s. However, no methods are known, which…
X-ray free-electron lasers (XFELs) offer unique capabilities for measuring the structure and dynamics of biomolecules, helping us understand the basic building blocks of life. Notably, high-repetition-rate XFELs enable single particle…
Understanding complex biological macromolecules, especially proteins, is vital for grasping their diverse chemical functions with direct impact in biology and pharmacology. While techniques like X-ray crystallography and cryo-electron…
The X-ray free electron lasers (XFEL) can enable diffractive structural determination of protein crystals or single molecules that are too radiation-sensitive for conventional X-ray analysis. However the electronic form factor could have…
Revealing the structure of complex biological macromolecules, such as proteins, is an essential step for understanding the chemical mechanisms that determine the diversity of their functions. Synchrotron based x-ray crystallography and…
We applied angular X-ray Cross-Correlation analysis (XCCA) to scattering images from a femtosecond resolution LCLS X-ray free-electron laser (XFEL) pump-probe experiment with solvated PtPOP ([Pt$_2$(P$_2$O$_5$H$_2$)$_4$]$^{4-}$) metal…
Here we propose to exploit the low energy bandwidth, small wavelength and penetration power of ultrashort pulses from XFELs for resonant Small Angle Scattering (SAXS) on plasma structures in laser excited plasmas. Small angle scattering…
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.…
Sub-angstrom spatial resolution of electron density coupled with sub-femtosecond temporal resolution is required to directly observe the dynamics of the electronic structure of a molecule after photoinitiation or some other ultrafast…
The advent of ultrafast pulsed X-ray free-electron lasers with very high brightness has enabled the determination of transient molecular structures of small and medium-sized organic molecules in excited states and undergoing chemical…