Browse our latest Structural Biology and Molecular Biophysics articles

Near atomic resolution of late 40S ribosomal subunit assembly by cryo-EM reveals immature rRNA active sites stabilized by biogenesis factors.

The super-resolution fluorescence microscopy approach polarization PALM (p-PALM) reveals that macromolecular crowding and inhomogeneity within nuclear pores generate a structurally and dynamically complex permeability barrier.

A high-resolution method to quantify interactions between lipid bilayers and single proteins under controlled load is presented and applied to key proteins involved in membrane fusion and formation and maintenance of membrane contact sites.

Integrative structural biology reveals a novel complex comprising the TATA-box-binding protein, TBP, and two subunits, TAF11 and TAF13, of General Transcription Factor TFIID, suggesting a new regulatory state in TFIID function in RNA polymerase II transcription initiation.

Six BBS proteins form a core BBSome transport vehicle, which is sufficient for recognizing membrane proteins for transport into the ciliary compartment.

Local sharpening of cryo-electron microscopy maps using atomic models can increase the interpretability of densities in cases of resolution variation and facilitates model building and refinement.

The structure of human PINK1 explains structural regulation and clarity on the impact of loss of function disease-associated mutations, which may stimulate future drug discovery efforts for both familial and idiopathic Parkinson's disease.

A combination of cryo-electron microscopy of TPX2 bound to microtubules and in vitro reconstitution experiments reveals a novel microtubule interaction mode that explains how TPX2 promotes microtubule nucleation and stabilization.

Mechanically stimulating mitochondria causes them to divide via the recruitment of the mitochondrial fission machinery to the mechanically strained site, showing that intracellular organelles can be mechanoresponsive.

Structural and biochemical studies of Kap123 revealed the mechanisms by which Kap123 recognizes H3- and H4-NLSs through two lysine-binding pockets and by which evolutionarily conserved diacetylation of H4-NLS facilitates Kap123-H3-NLS mediated nuclear translocation.