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A novel strategy is presented for quantitatively measuring protein-DNA and protein-protein interactions that regulate transcription in living cells.

The rate of DNA unwinding by RecQ helicases is dramatically modulated by the DNA duplex stability in a geometry-dependent manner, providing an intrinsic mechanism for suppressing illegitimate recombination.

The identification of a single-CD4 bound asymmetric HIV-1 Envelope trimer intermediate provides new mechanistic insights into the activation of Envelope for fusion, and highlights the importance of asymmetry in biology.

The mechanical stability of a nucleosome is enhanced upon the introduction of a single base pair mismatch that makes DNA more bendable, with implications on mismatch repair in vivo.

The combined use of optical trapping and single-molecule FRET permits the study of riboswitch structure formation and conformational dynamics at the same time.

Upon DNA damage, Rad52 forms a membraneless sub-compartment where Rad52 molecules are highly dynamic and share properties with liquid-liquid phase-separated molecules, reflecting the existence of a liquid droplet around damaged DNA.

In vivo single-molecule imaging demonstrates that Smc5/6 chromatin association depends on ATP hydrolysis and dsDNA binding, requires Nse6 and is modulated by Brc1 after DNA damage.

A new analysis algorithm (DISC) enables accurate analysis of data from high-throughput single-molecule paradigms and reveals a non-cooperative binding mechanism of cyclic nucleotide-binding domains from HCN ion channels.

Single-molecule localization imaging shows that the Nipah virus fusion protein forms nanoscale clusters on cell and viral membranes that favor membrane fusion activation.

In vitro single-particle tracking reveals that ATP binding increases the one-dimensional diffusion of yeast chromatin remodeler SWR1 on DNA stretched between optical tweezers and diffusion is confined by protein roadblocks and nucleosomes.