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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…
Emerging coherent X-ray scattering patterns of single particles have shown dominant morphological signatures in agreement with predictions of the scattering model used for conventional protein crystallography. The key question is if and to…
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.…
We describe a diffraction microscopy technique based on refractive optics to study structural variations in crystals. The X-ray beam diffracted by a crystal was magnified by beryllium parabolic refractive lenses on a 2D X-ray camera. The…
Cryo-electron tomography enables 3D visualization of cells in a near native state at molecular resolution. The produced cellular tomograms contain detailed information about all macromolecular complexes, their structures, their abundances…
The classical method of determining the atomic structure of complex molecules by analyzing diffraction patterns is currently undergoing drastic developments. Modern techniques for producing extremely bright and coherent X-ray lasers allow a…
Crystalline phase structure is essential for understanding the performance and properties of a material. Therefore, this study identified and quantified the crystalline phase structure of a sample based on the diffraction pattern observed…
In the effort to aid cytologic diagnostics by establishing automatic single cell screening using high throughput digital holographic microscopy for clinical studies thousands of images and millions of cells are captured. The bottleneck lies…
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…
Emerging coherent X-ray scattering patterns of single-particles have shown dominant morphological signatures in agreement with predictions of the scattering model used for conventional protein crystallography. The key question is if and to…
Single-particle cryo-electron microscopy (cryo-EM) has recently joined X-ray crystallography and NMR spectroscopy as a high-resolution structural method to resolve biological macromolecules. In a cryo-EM experiment, the microscope produces…
The formation of a viral capsid -- the highly-ordered protein shell that surrounds the genome of a virus -- is the canonical example of self-assembly. The capsids of many positive-sense RNA viruses spontaneously assemble from in vitro…
Multi-technique high resolution X-ray mapping enhanced by the recent advent of 4th generation synchrotron facilities can produce colossal datasets, challenging traditional analysis methods. Such difficulty is clearly materialized when…
Cryo-electron microscopy (cryo-EM) is a powerful technique for determining the structure of proteins and other macromolecular complexes at near-atomic resolution. In single particle cryo-EM, the central problem is to reconstruct the…
X-ray as well as electron diffraction are powerful tools for structure determination of molecules. Studies on randomly oriented molecules in the gas-phase address cases in which molecular crystals cannot be generated or the interaction-free…
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.…
A fundamental goal of research in molecular biology is to understand protein structure. Protein crystallography is currently the most successful method for determining the three-dimensional (3D) conformation of a protein, yet it remains…
We present here an overview of Coherent X-ray Diffraction Imaging (CXDI) with its application to nanostructures. This imaging approach has become especially important recently due to advent of X-ray Free-Electron Lasers (XFEL) and its…
Established x-ray diffraction methods allow for high-resolution structure determination of crystals, crystallized protein structures or even single molecules. While these techniques rely on coherent scattering, incoherent processes like…
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…