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.
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.
An atomic model of the bacterial chemosensory array obtained through the synthesis of cryo-electron tomography and large-scale molecular-dynamics simulations reveals a new kinase conformation during signaling events.
The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.
Fiducial-less tomography on single particle cryoEM samples reveals that most particles are adsorbed to the air-water interface and allows for researchers to diagnose and solve sample, grid, ice thickness, collection, and processing issues.
Cryo-electron tomography unveils striking new structural components of positive-strand virus RNA replication compartments, greatly advancing mechanistic insights into the structure, assembly, function and control of these critical complexes.