Kindai University

Super-resolution imaging flow cytometry (SR-IFC) brings structured-illumination microscopy into a continuous microfluidic stream: each cell yields only three phase-shifted frames, physical modulation sharpens the flow axis, and a network trained solely on the imaged sample's own data infers the missing transverse detail. On 100 nm fluorescent beads, SR-IFC reached about 118 nm along the flow axis and 110 nm across it, versus 222 to 227 nm for wide-field imaging of the same beads; with a 2048 × 320 pixel readout, the theoretical throughput ceiling is about 720 cells per second.

Super-resolution imaging flow cytometry (SR-IFC) brings structured-illumination microscopy into a continuous microfluidic stream: each cell yields only three phase-shifted frames, physical modulation sharpens the flow axis, and a network trained solely on the imaged sample's own data infers the missing transverse detail. On 100 nm fluorescent beads, SR-IFC reached about 118 nm along the flow axis and 110 nm across it, versus 222 to 227 nm for wide-field imaging of the same beads; with a 2048 × 320 pixel readout, the theoretical throughput ceiling is about 720 cells per second.

Molecular dynamics trajectories no longer have to be read only through per-residue fluctuations. Low-population, state-dependent coupling signals were previously hard to separate from high-dimensional trajectories. After compressing each residue pair's side-chain heavy-atom mean-distance time series into a 25-dimensional latent space, then clustering and building networks, the ligand-bound state is dominated by lid residue pairs, while the SAVI-associated multi-mutant shifts to an a1b1-enriched, cross-protomer organization involving residue 281.

Molecular dynamics trajectories no longer have to be read only through per-residue fluctuations. Low-population, state-dependent coupling signals were previously hard to separate from high-dimensional trajectories. After compressing each residue pair's side-chain heavy-atom mean-distance time series into a 25-dimensional latent space, then clustering and building networks, the ligand-bound state is dominated by lid residue pairs, while the SAVI-associated multi-mutant shifts to an a1b1-enriched, cross-protomer organization involving residue 281.