Neocortical synapses in layer 4 of the human temporal lobe neocortex were quantitatively characterized, at the subcellular level, using high-end, high-resolution electron microscopy and 3D-volume reconstructions.
Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.
Cryo-EM structure of monomeric human Frizzled5 was determined with a universal fiducial antibody at 3.7 Å overall resolution, which supports a simple Fzd/LRP6 heterodimerization mechanism of canonical Wnt/β-catenin signaling.
Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
Structures of the signal recognition particle before and after it captures a transmembrane domain suggest how it chooses, engages, and shields its clients during membrane protein targeting to the endoplasmic reticulum.