Publications by authors named "T Gonen"
Article Synopsis
- Microcrystal electron diffraction (MicroED) is an advanced structural method useful for analyzing a variety of samples, including small molecules and proteins, using cryogenic electron microscopy techniques.
- The method captures diffraction data through the continuous rotation of small 3D crystals while being observed by a high-speed camera, then utilizes X-ray crystallographic software for structure determination.
- This guide provides detailed protocols for preparing samples, emphasizing that individual crystals need tailored growth conditions, and aids those with backgrounds in biochemistry and crystallography in optimizing their MicroED experiments, which can take from one day to several weeks.
Virus-induced cellular condensates, or viral factories, are poorly understood high-density phases where replication of many viruses occurs. Here, by cryogenic electron tomography (cryoET) of focused ion beam (FIB) milling-produced lamellae of mammalian reovirus (MRV)-infected cells, we visualized the molecular organization and interplay (i.e.
View Article and Find Full Text PDFTwo patients, a 38-year-old woman and, a 74-year-old man, had ulceronodular basal cell carcinoma at the lower eyelid margin, directly opposite a nodular intradermal nevus at the upper lid margin. Both patients had the nevi for decades and the tumors for 2 and 3 years, respectively. The size of the tumors were 9 × 4 mm and 10 × 15 mm.
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- Scientists studied a medicine called fluticasone, which helps with allergies and breathing problems, but didn't know how it looks in 3D for a long time.
- *They used a special technique called MicroED to figure out its 3D shape and how it changes in different states, like in a drug form or in our body.
- *The research shows that tiny changes in fluticasone's structure can affect how well it works, making it important for understanding how medicines help us.
High resolution information is important for accurate structure modelling. However, this level of detail is typically difficult to attain in macromolecular crystallography because the diffracted intensities rapidly fade with increasing resolution. The problem cannot be circumvented by increasing the fluence as this leads to detrimental radiation damage.
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