Related papers: High-Resolution Structure of Viruses from Random S…

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, known for its ability to reveal internal structures of objects, is expected to provide richer information for 3D reconstruction than visible light. Yet, existing neural radiance fields (NeRF) algorithms overlook this important nature…

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…

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 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 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.…

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…

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…

High-quality total scattering data, a key tool for understanding atomic-scale structure in disordered materials, require stable instrumentation and access to high momentum transfers. This is now routine at dedicated synchrotron…

X-ray fluorescence (XRF) enables element-specific, nondestructive imaging, but conventional raster scanning scales poorly with sample size, particularly for tomography, because measurements must be repeated at every projection angle and…

We reconstructed intensities in Fourier space and electron densities in the real space for an azimuthally symmetric object Nanorice particle (Iron Oxide nanoparticle) exposed in the ultrashort, bright and coherent x-ray free electron laser…

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…

The structure and dynamics of isolated nanosamples in free flight can be directly visualized via single-shot coherent diffractive imaging using the intense and short pulses of X-ray free-electron lasers. Wide-angle scattering images even…

Optical tomographic reconstruction of a 3D nanoscale specimen is hindered by the axial diffraction limit, which is 2-3 times worse than the focal plane resolution. We propose and experimentally demonstrate an axial super-resolution…

X-ray Absorption Spectroscopy (XAS) is a widely used X-ray diagnostic method. While synchrotrons have large communities of XAS users, its use on X-Ray Free Electron Lasers (XFEL) facilities has been rather limited. At a first glance, the…

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…

A modulated icosahedral shell with an inclusion is a concise description of many viruses, including recently-discovered large double-stranded DNA ones. Many X-ray scattering patterns of such viruses show major polygonal fringes, which can…

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…

Serial femtosecond X-ray crystallography (SFX) captures the structure and dynamics of biological macromolecules at high spatial and temporal resolutions. The ultrashort pulse produced by an X-ray free electron laser (XFEL) 'outruns' much of…

The ingenious idea of single molecule imaging by hard x-ray Free Electron Laser (X-FEL) pulses was recently proposed by Neutze et al. [Nature,406,752(2000)]. However, in their numerical modelling of the Coulomb explosion several…