Nature Structural & Molecular Biology, Published online: 14 September 2026; doi:10.1038/s41594-026-01885-6Ciapponi et al. determine the cryo-electron microscopy structure of the canonical Polycomb repressive complex 1 holocomplex and show how its architecture coordinates complex assembly, H2A monoubiquitination and genomic targeting.

Bacterial Exotoxin B proteins are typically binary pore-forming toxins. Here, authors characterise Vpb4, a homologue from entomopathogenic Bacillus thuringiensis, and reveal the structural basis enabl...

An optical archival storage technology based on femtosecond laser direct writing in glass addresses the practical demands of archival storage.

The emergence of a chemical system capable of self-replication and evolution is a critical event in the origin of life. RNA polymerase ribozymes can replicate RNA, but their large size and structural ...

Nature Structural & Molecular Biology, Published online: 12 February 2026; doi:10.1038/s41594-026-01746-2Tafur et al. determined the cryo-electron microscopy structure of the SEA complex (GATOR) bound to its substrate, the EGO complex (Ragulator–Rag), and showed that its GAP activity is essential for both rapid inactivation and reactivation of TORC1.

Sidewinder enables high-fidelity DNA assembly by separating the information that guides assembly from the final assembled sequence.

Nine in 10 Australian researchers had their “ideas grant” applications rejected last year, even as Australia’s medical investment fund sits on $5 billion more than it was designed to hold.

This study reveals how KICSTOR and GATOR1 assemble into a crescent-shaped lysosomal complex that regulates mTORC1 during amino acid starvation and how SAMTOR binds KICSTOR in an S-adenosylmethionine-incompatible conformation to couple methionine sensing to mTORC1 regulation.