Imaging a material with electrons at near-atomic resolution requires a thin specimen that is
stable in the vacuum of the transmission electron microscope. For biological samples, this …

Single-particle cryo-electron microscopy (cryo-EM SPA) has recently emerged as an
exceptionally well-suited technique for determining the structure of membrane proteins …

Single particle cryo-electron microscopy (cryoEM) is often performed under the assumption
that particles are not adsorbed to the air-water interfaces and in thin, vitreous ice. In this …

The increasing demand for cryo-electron microscopy (cryo-EM) reveals drawbacks in current
sample preparation protocols, such as sample waste and lack of reproducibility. Here, we …

Low-dose images obtained by electron cryo-microscopy (cryo-EM) are often affected by
blurring caused by sample motion during electron beam exposure, degrading signal …

Microtubules are nucleated in vivo by γ-tubulin complexes. The 300-kDa γ-tubulin small
complex (γ-TuSC), consisting of two molecules of γ-tubulin and one copy each of the …

Almost every aspect of cryo electron microscopy (cryoEM) has been automated over the last
few decades. One of the challenges that remains to be addressed is the robust and reliable …

Nine different near-atomic resolution structures of icosahedral viruses, determined by
electron cryo-microscopy and published between early 2008 and late 2010, fulfil predictions …

Aqueous biological samples must be “preserved”(stabilized) before they can be placed in
the high vacuum of an electron microscope. Among the various approaches that have been …

The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γγTuRC is
assembled from repeating γγ-tubulin small complex (γTuSC) subunits and is thought to …