Related papers: High-resolution structure of viruses from random d…
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…
Recovery of three-dimensional structure from single particle X-ray scattering of completely randomly oriented diffraction patterns as predicted few decades back has been real due to the advent of the new emerging X-ray Free Electron Laser…
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…
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…
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…
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…
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…
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…
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…
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…
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…
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…
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…
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.…
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…
Modern technology for producing extremely bright and coherent X-ray laser pulses provides the possibility to acquire a large number of diffraction patterns from individual biological nanoparticles, including proteins, viruses, and DNA.…
Theory predicts that with an ultrashort and extremely bright coherent X-ray pulse, a single diffraction pattern may be recorded from a large macromolecule, a virus, or a cell before the sample explodes and turns into a plasma. Here we…
Single biomolecular imaging using XFEL radiation is an emerging method for protein structure determination using the "diffraction before destruction" method at near atomic resolution. Crucial parameters for such bio-imaging experiments are…
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…