Scientific Highlights from Research Division
Photon Science (PSD)
Catalysts used in industry change their material structure over the years. Using a new method, PSI researchers have now studied this on the nanoscale.
Crystal structure of SARS-CoV-2 Orf9b in complex with human TOM70 suggests unusual virus-host interactions
In a study published in Nature Communications, researchers at the NHC Key Laboratory of Systems Biology of Pathogens in Beijing, China, in collaboration with the Paul Scherrer Institut characterize the interactions of SARS-CoV-2 orf9b and human TOM70 biochemically, and they determine the 2.2 Å crystal structure of the TOM70 cytosolic domain with a bound SARS-CoV-2 orf9b peptide.
Breakthrough applications of high-resolution and high-counting statistics synchrotron X-Ray Powder Diffraction to protein powders leading to the determination of a 1.8 structural model of the pharmaceutical peptide "octreotide" - the highest resolution ever achieved for a peptide of this complexity using X-ray powder diffraction and crystallographic methods.
Microrobots, materials with shape memory, and better particle accelerators are made possible through the exploration of magnetism at PSI.
Myelin 'insulates' our neurons enabling fast signal transduction in our brain. Myelin levels, integrity, and neuron orientations are important determinants of brain development and disease. Small-angle X-ray scattering tensor tomography (SAXS-TT) is a promising technique for non-destructive, stain-free imaging of brain samples, enabling quantitative studies of myelination and neuron orientations, i.e. of nano-scale properties imaged over centimeter-sized samples.
Light is essential for life, and for researchers it is also a wonderful tool to better understand the structure of materials.
Researchers at Goethe University Frankfurt, in cooperation with the PSI have probably discovered another, previously unknown mechanism of action of the antiviral remdesivir.
Using a combination of computer simulations and laboratory experiments, PSI researchers have identified new binding sites for active agents on the vital protein tubulin.
Detailed characterization of the tooth and jaw structure and development among shark ancestors by synchrotron based X-ray tomographic microscopy at TOMCAT led an international team of researchers from the Naturalis Biodiversity Center in Leiden and the University of Bristol to the discovery that while teeth evolved once, complex dentitions have been gained and lost many times in evolutionary history.