Cryo–electron microscopy, or simply cryo-EM, refers mainly to three very different yet closely
related techniques: electron crystallography, single-particle cryo-EM, and electron …

For many years, structure determination of biological macromolecules by cryo-electron
microscopy (cryo-EM) was limited to large complexes or low-resolution models. With recent …

Abstract α-Synuclein (aSyn) fibrillar polymorphs have distinct in vitro and in vivo seeding
activities, contributing differently to synucleinopathies. Despite numerous prior attempts, how …

Advances in high-resolution cryo-electron microscopy (cryo-EM) require the development of
validation metrics to independently assess map quality and model geometry. We report …

Recent advances in single-particle cryoelecton microscopy (cryo-EM) are enabling
generation of numerous near-atomic resolution structures for well-ordered protein …

Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Transient receptor potential (TRP) channels are sensors for a wide range of cellular and
environmental signals, but elucidating how these channels respond to physical and …

In recent work with large high-symmetry viruses, single-particle electron cryomicroscopy
(cryo-EM) has achieved the determination of near-atomic-resolution structures by allowing …

Until only a few years ago, single-particle electron cryo-microscopy (cryo-EM) was usually
not the first choice for many structural biologists due to its limited resolution in the range of …

Abstract Three-dimensional (3D) structure determination by single particle electron
cryomicroscopy (cryoEM) involves the calculation of an initial 3D model, followed by …