Low-dose cryo-electron ptychography of proteins at sub-nanometer resolution.

Cryo-transmission electron microscopy (cryo-EM) of frozen hydrated specimens is an efficient method for the structural analysis of purified biological molecules. However, cryo-EM and cryo-electron tomography are limited by the low signal-to-noise ratio (SNR) of recorded images, making detection of smaller particles challenging. For dose-resilient samples often studied in the physical sciences, electron ptychography - a coherent diffractive imaging technique using 4D scanning transmission electron microscopy (4D-STEM) - has recently demonstrated excellent SNR and resolution down to tens of picometers for thin specimens imaged at room temperature.

[Passporting of parents of disabled children as an analytical resource of social policy].

The article presents the results of a study of the main social and household characteristics of families with disabled children, conducted in the territory of the Belgorod region (targeted survey; n = 990). The research made it possible to answer questions about children's health problems, their living conditions, the economic status of the family, the work of parents, the social environment and other characteristics of families. The article examines the passporting method of target problem (socially vulnerable) groups as an effective way of obtaining system information, a social picture of the situation, conditions, and problems of such families.

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates.

Tau protein fibrillization is implicated in the pathogenesis of several neurodegenerative diseases collectively known as Tauopathies. For decades, investigating Tau fibrillization in vitro has required the addition of polyanions or other co-factors to induce its misfolding and aggregation, with heparin being the most commonly used. However, heparin-induced Tau fibrils exhibit high morphological heterogeneity and a striking structural divergence from Tau fibrils isolated from Tauopathies patients' brains at ultra- and macro-structural levels.