Jun 22, 2022 · Here we present a high-resolution cryo-electron microscopy (cryo-EM) structure of a 2.8 megadalton T4SS complex composed of 92 polypeptides representing 8 of the 10 essential T4SS components...

Apr 3, 2024 · Here we discuss how the interplay between cryo-EM and cryo-electron tomography, as a connecting bridge to visualize macromolecules in situ, holds great promise to create comprehensive...

May 13, 2022 · Here, we report the cryo-EM structures of human GLUT4 bound to a small molecule inhibitor cytochalasin B (CCB) at resolutions of 3.3 Å in both detergent micelles and lipid nanodiscs. CCB-bound...

The 3.8Å cryo-EM structure of the mature Zika virus revealed the arrangement of 180 envelope glycoproteins forming the icosahedral shell and highlighted unique features near the Asn154 glycosylation site, distinct from other flaviviruses. This site, visible in the cryo-EM density, likely plays a crucial role in host cell binding and entry ...

Jan 20, 2022 · This review summarizes the current state of methods and results achievable by cryo-electron microscopy (cryo-EM) imaging for molecular, cell, and structural biologists who wish to understand what is required and how it might help to address their research questions.

In this article, the principle, characteristics, history, current situation, workflow, and common problems of cryo‐EM are systematically reviewed. In addition, the new development direction of cryo‐EM—cryo‐electron tomography (cryo‐ET), is discussed in detail.

5 days ago · Our cryo-EM structure supported the previous prediction from cross-linking and structural analyses that the polypeptide ligand interacts with the edge strand of the MREβ sheet by the strand addition mechanism. Because of the low resolution of density maps and the absence of secondary structure restraints in the refinement in our cryo-EM ...

Here, we present the cryo–electron microscopy structure of the outward open conformation of the rat peptide transporter PepT2 in complex with an inhibitory nanobody.

Jan 24, 2024 · Here, we report the cryogenic electron microscopy (cryo-EM) structure of an active PR, specifically the complete, heterodimeric TPR apoenzyme determined at its optimal functional magnesium ion concentration ( [Mg 2+] = 100 mM), augmented by a comprehensive fitness landscape of TPR function.

Cryo-EM plays an important role in revealing the structures underlying these processes. For example, the Kirchdoerfer group used cryo-EM to reconstruct the polymerase of an alphacoronavirus called porcine epidemic diarrhea virus — a global pathogen that is particularly fatal for neonatal piglets.