Single-particle cryogenic electron microscopy (cryo-EM) has emerged as a powerful
technique to visualize the structural landscape sampled by a protein complex. However …

During assembly, ribosomal particles in bacteria fold according to energy landscapes
comprised of multiple parallel pathways. Cryo-electron microscopy studies have identified a …

Assembly of ribosomes in bacteria is highly efficient, taking~ 2-3 min, but this makes the
abundance of assembly intermediates very low, which is a challenge for mechanistic …

Cryo-electron tomography (cryo-ET) enables observation of macromolecular complexes in
their native, spatially contextualized cellular environment. Cryo-ET processing software to …

AAA+ proteolytic machines unfold proteins before degrading them. Here, we present cryoEM
structures of ClpXP-substrate complexes that reveal a postulated but heretofore unseen …

AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for
example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize …

FtsH, a AAA protease, associates with HflK/C subunits to form a megadalton complex that
spans the inner membrane and extends into the periplasm of E. coli. How this complex and …

30S subunits become inactive upon exposure to low Mg2+ concentration, because of a
reversible conformational change that entails nucleotides (nt) in the neck helix (h28) and 3 …

Throughout the history of electron microscopy, ribosomes have served as an ideal subject
for imaging and technological development, which in turn has driven our understanding of …

Rapid structural analysis of purified proteins and their complexes has become increasingly
common thanks to key methodological advances in cryo-electron microscopy (cryo-EM) and …