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.
Specific attachment of molecularly defined gold nanoparticles enables precise localization, critical for structural studies in vivo, of proteins of unknown structure within the cellular milieu by cryo-electron tomography.
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.