Publications by authors named "O M Yefanov"
High-resolution X-ray imaging of noncrystalline objects is often achieved through the approach of scanning coherent diffractive imaging known as ptychography. The imaging resolution is usually limited by the scattering properties of the sample, where weak diffraction signals at the highest scattering angles compete with parasitic scattering. Here, we demonstrate that X-ray multilayer Laue lenses with a high numerical aperture (NA) can be used to create a strong reference beam that holographically boosts weak scattering from the sample over a large range of scattering angles, enabling high-resolution imaging that is tolerant of such background.
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- * Recent advancements in the field include the approval of boronate-based β-lactamase inhibitors for treating multidrug-resistant bacteria, emphasizing the need for effective solutions.
- * Researchers used time-resolved serial crystallography to gain insights into the binding mechanisms of β-lactamase CTX-M-14, collecting detailed data that enhances the understanding of enzymatic reactions and resistance.
Multilayer Laue lenses are volume diffractive optical elements for hard X-rays with the potential to focus beams to sizes as small as 1 nm. This ability is limited by the precision of the manufacturing process, whereby systematic errors that arise during fabrication contribute to wavefront aberrations even after calibration of the deposition process based on wavefront metrology. Such aberrations can be compensated by using a phase plate.
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- The main protease (M) of SARS-CoV-2 is crucial for the virus's functionality and is considered a potential target for drug development, as it is only active in its reduced form.
- When oxidized, M's activity halts but can be restored, indicating an evolutionary adaptation to oxidative environments, although the protective mechanisms haven't been fully elucidated.
- Researchers determined the crystal structure of oxidized M, revealing a disulfide bond that affects its dimer stability and crystallization, providing insights into the protein's response to oxidative stress and its structural study conditions.*
Serial crystallography (SX) has become an established technique for protein structure determination, especially when dealing with small or radiation-sensitive crystals and investigating fast or irreversible protein dynamics. The advent of newly developed multi-megapixel X-ray area detectors, capable of capturing over 1000 images per second, has brought about substantial benefits. However, this advancement also entails a notable increase in the volume of collected data.
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