All-atom molecular dynamics of the HBV capsid supports a role for structural asymmetry in biological function, reveals the potential for triangular pores to mediate cellular signaling, and indicates that capsid flexibility may limit resolution attainable by cryo-EM.
Cryo-EM structures of actomyosin VI in multiple nucleotide states reveal a unique actin-myosin interface and a mechanism of force-sensitivity; furthermore, myosin VI remodels F-actin, suggesting a role for actin structural plasticity during force generation.
The Volta phase plate enables in-focus single particle analysis at near atomic resolutions, which could expand the capabilities of cryo-EM, especially for small, flexible or heterogeneous macromolecular samples.
Building on previous work in cryo-electron microscopy (Entchev et al, 2015), it shown that a combination of the Volta phase plate and a small amount of defocus can simplify the experimental set-up, increase the data acquisition rate and improve resolution.
Structures of the replicative DNA polymerase Pol IIIα, the DNA sliding clamp, the proofreading exonuclease, and the processivity switch Tau (τ) suggest a mechanism for quick release during lagging strand synthesis.