Jacqueline L. S. Milne

TL;DR: The structure of a complex between Escherichia coli β-galactosidase and the cell-permeant inhibitor phenylethyl β-d-thiogalactopyranoside is determined by cryo-EM at an average resolution of ~2.2 angstroms, demonstrating that preparation of specimens of adequate quality and intrinsic protein flexibility now represent the major bottlenecks to routinely achieving resolutions close to 2 Å using single-particle cryo

TL;DR: Two perceived barriers in single-particle cryo-EM are overcome: crossing 2 Å resolution and obtaining structures of proteins with sizes with sizes < 100 kDa, demonstrating that crye-EM can be used to investigate a broad spectrum of drug-target interactions and dynamic conformational states.

TL;DR: Cryo-EM structures establish the sequence of nucleotide-driven structural changes in p97 at atomic resolution and enable elucidation of the binding mode of an allosteric small-molecule inhibitor to p97 and illustrate how inhibitor binding at the interface between the D1 and D2 domains prevents propagation of the conformational changes necessary for p97 function.

TL;DR: An overview of emerging themes in the application of this technology to investigate diverse questions in biology and medicine is provided, including a description of how the structural information obtained by cryo‐EM is deposited and archived in a publicly accessible database.

TL;DR: A structural signature of the open Env conformation is a three-helix motif composed of α-helical segments derived from highly conserved, non-glycosylated N-terminal regions of the gp41 trimer, suggesting a new structural template for designing immunogens that can elicit antibodies targeting HIV at a vulnerable, pre-entry stage.