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ChemSystemsChem 3(3), e2000050 (2021). doi:10.1002/syst.202000050, Huntington's disease (HD) is one of nine neurodegenerative disorders associated with an extension of polyglutamine (polyQ) in proteins. In HD, the polyQ tract in the huntingtin protein is extended beyond a threshold of 38 amino acids leading to the formation of amyloidal structures in the cytoplasm and nucleus. We investigated here the structure of Htt (Huntingtin) amyloid fibrils in cellulo with nanoprobe small angle X-ray scattering. As these measurements were performed under cryogenic conditions, the information is obtained on the aggregates in their natural, hydrated environment without the need of staining and chemical fixation. We also could show the presence of oligomer structures not visible in fluorescence microscopy. Structural information on repetitive units inside of Htt inclusion bodies was determined from the SAXS data and compared to electron microscopy images. The results suggest that nanoprobe cryo-SAXS can serve as powerful tool to investigate the kinetics of amyloid aggregate formation inside cells and to understand how fibril formation can be influenced by drugs and other external stimuli., Published by Wiley-VCH Verlag, Weinheim

Ptychographic imaging with soft X-rays, especially in the water window energy range, suffers from limited detector dynamic range that directly influences the maximum spatial resolution achievable. High-dynamic-range data can be obtained by multiple exposures. By this approach we have increased the dynamic range of a ptychographic data set by a factor of 76 and obtained diffraction signal till the corners of the detector. The real space half period resolution was improved from 50 nm for the single exposure data to 18 nm for the high-dynamic-range data., Comment: 4 pages, 3 figures, Proceedings of XRM-2016 Conference, Oxford, UK