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The advent of the X-ray Free Electron Laser (XFEL) has made it possible to record diffraction snapshots of biological entities injected into the X-ray beam before the onset of radiation damage. Algorithmic means must then be used to…
The advent of the X-ray Free Electron Laser (XFEL) has made it possible to record snapshots of biological entities injected into the X-ray beam before the onset of radiation damage. Algorithmic means must then be used to determine the…
The study of the structure of viruses by X-ray free-electron lasers (XFEL) attracts more attention in recent decades. Such experiments are based on the collection of two-dimensional diffraction patterns measured at the detector after…
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…
The first experimental data from single-particle scattering experiments from free electron lasers (FELs) are now becoming available. The first such experiments are being performed on relatively large objects such as viruses, which produce…
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…
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…
Conventional X-ray methods use incoming plane waves and result in discrete diffraction patterns when scattered at crystals. Here we find, by a systematic method, incoming waveforms which exhibit discrete diffraction patterns when scattered…
Single-shot wide-angle diffraction imaging is a widely used method to investigate the structure of non-crystallizing objects such as nanoclusters, large proteins or even viruses. Its main advantage is that information about the…
Single particle imaging (SPI) at X-ray free electron lasers (XFELs) is a technique to determine the 3D structure of nanoscale objects like biomolecules from a large number of diffraction patterns of copies of these objects in random…
Modern Flash X-ray diffraction Imaging (FXI) acquires diffraction signals from single biomolecules at a high repetition rate from X-ray Free Electron Lasers (XFELs), easily obtaining millions of 2D diffraction patterns from a single…
A new scheme based on (i) upcoming brilliant X-ray Free Electron Laser (FEL) sources, (ii) novel energy and angular dispersive, large-area electron imagers and (iii) the well-known photoelectron holography is elaborated that provides…
Schemes for X-ray imaging single protein molecules using new x-ray sources, like x-ray free electron lasers (XFELs), require processing many frames of data that are obtained by taking temporally short snapshots of identical molecules, each…
The advent of X-ray free-electron lasers (XFELs) has revolutionized fundamental science, from atomic to condensed matter physics, from chemistry to biology, giving researchers access to X-rays with unprecedented brightness, coherence, and…
The routine atomic-resolution structure determination of single particles is expected to have profound implications for probing the structure-function relationship in systems ranging from energy materials to biological molecules.…
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…
Ultrafast X-ray imaging provides high resolution information on individual fragile specimens such as aerosols, metastable particles, superfluid quantum systems and live biospecimen, which is inaccessible with conventional imaging…
Since Perutz, Kendrew and colleagues unveiled the structure of hemoglobin and myoglobin based on X-ray diffraction analysis in the 1950s, X-ray crystallography has become the primary methodology used to determine the 3D structure of…
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…
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…