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Crystal structures of the linker region of TRPML1 reveal that the luminal domain forms a tetrameric pore. Along with electrophysiology studies, this work provides insight into the mechanism of channel regulation by Ca2+ and H+.
The cryo-EM structure of pre-60S purified via Nmd3 provides molecular insights into the roles of assembly factors Nmd3, Lsg1, Tif6 and Reh1 in the last steps of ribosomal large-subunit maturation.
A comprehensive analysis of the human SUMO proteome, in HeLa and U2OS cell lines and under different conditions, identifies new SUMOylated sites and reveals cross-talk between SUMO and other post-translational modifications, such as phosphorylation.
Crystal structures of a localization element of ASH1 mRNA alone, in complex with its nuclear shuttling protein She2p, and in the cytoplasmic complex with She2p and She3p reveal a step-wise maturation pathway.
Cryo-EM structures of full-length human PC2 reveal two distinct channel states: an open conformation and a blocked conformation with Ca2+ bound at the entrance of the selectivity filter.
The cryo-EM structure of immature Zika virus shows partially ordered capsid proteins and reveals differences between pre-epidemic and epidemic strains at protein interfaces within the trimeric spikes.
A combination of SILAC-MS, genome-wide nucleosome mapping and live-cell imaging reveal rapid histone degradation and global chromatin decompaction after the induction of DNA double-strand breaks in S. cerevisiae.
The yeast ribosome-associated complex (RAC) is formed by Hsp40 protein Zuo1 and the atypical Hsp70 chaperone Ssz1. Structural analyses show Ssz1 in a hybrid conformation between the open and closed state and its substrate-binding domain completed by Zuo1.
Cryo-EM structures of secretin GspD in type II secretion systems from Escherichia coli and Vibrio cholera reveal a pentadecameric architecture, with three rings in the periplasm and β-strand-enriched gates on the outer membrane.
Cryo-EM and NMR analyses of the E. coli replisome show how DNA-end fraying after mismatch incorporation at the polymerase active site enables substrate ends to reach the ‘proofreading’ exonuclease site for mismatch removal.