Related papers: Reference-enhanced X-ray Single Particle Imaging
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…
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…
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.…
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,…
We present a novel method for Ankylography: three-dimensional structure reconstruction from a single shot diffraction intensity pattern. Our approach allows reconstruction of objects containing many more details than was ever demonstrated,…
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…
While the implementation of single particle coherent diffraction imaging for non-crystalline particles is complicated by current limitations in photon flux, hit rate, and sample delivery a concept of many-particle coherent diffraction…
A solution to the inversion problem of scattering would offer aberration-free diffraction-limited 3D images without the resolution and depth-of-field limitations of lens-based tomographic systems. Powerful algorithms are increasingly being…
X-ray ptychography is one of the versatile techniques for nanometer resolution imaging. The magnitude of the diffraction patterns is recorded on a detector and the phase of the diffraction patterns is estimated using phase retrieval…
Single particle cryo-electron microscopy is a vital tool for 3D characterization of protein structures. A typical workflow involves acquiring projection images of a collection of randomly oriented particles, picking and classifying…
We introduce a single-frame diffractive imaging method called randomized probe imaging (RPI). In RPI, a sample is illuminated by a structured probe field containing speckles smaller than the sample's typical feature size. Quantitative…
In nuclear arms control and disarmament processes, it is crucial to determine whether an object is a nuclear weapon or not without revealing sensitive information about it. At the MIT: Laboratory for Nuclear Security and Policy, such a…
Single-shot ptychography is a quantitative phase imaging method wherein overlapping beams of light arranged in a grid pattern simultaneously illuminate a sample, allowing a full ptychographic dataset to be collected in a single shot. It is…
Single-shot X-ray imaging of short-lived nanostructures such as clusters and nanoparticles near a phase transition or non-crystalizing objects such as large proteins and viruses is currently the most elegant method for characterizing their…
Coherent diffraction imaging is a high-resolution imaging technique whose potential can be greatly enhanced by applying the extrapolation method presented here. We demonstrate enhancement in resolution of a non-periodical object…
Coherent X-ray diffraction microscopy is a method of imaging non-periodic isolated objects at resolutions only limited, in principle, by the largest scattering angles recorded. We demonstrate X-ray diffraction imaging with high resolution…
Single-particle electron cryomicroscopy (cryo-EM) is an increasingly popular technique for elucidating the three-dimensional structure of proteins and other biologically significant complexes at near-atomic resolution. It is an imaging…
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…
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…
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…