Single particle cryo-electron microscopy (cryo-EM) is an emerging powerful tool for structural studies of macromolecular assemblies (i.e., protein complexes and viruses). Although single particle cryo-EM requires less concentrated and smaller amounts of samples than X-ray crystallography, it remains challenging to study specimens that are low-abundance, low-yield, or short-lived. The recent dev...

In cryo-electron microscopy (cryo-EM), vitreously frozen biological specimens can tolerate only a limited electron dose for imaging. Therefore, cryo-EM micrographs display weak contrast and a poor signal-to-noise ratio. This limits data interpretability and prevents efficient application of cryo-EM to a wider range of biological problems. Continued efforts have been invested in imaging methods ...

INTRODUCTION Catheter ablation of paroxysmal AF using the Cryoballoon (CRYO) has yielded similar success rates to conventional wide encirclement using radiofrequency catheter ablation (RFCA), but randomized data are lacking. Pilot data suggested a high success rate with a combined approach (COMBINED) using wide encirclement with RFCA followed by 2 CRYO applications to each vein. We compared the...

Cryo-electron microscopy (Cryo-EM) and cryo-electron tomography (Cryo-ET) provide structural insights into complex biological processes. The podoviridae are dsDNA containing phage with short, non-contractile tails which nevertheless translocate their DNA into the cytoplasm of their host cells. Liu et al. [1] used a combination of cryo-EM and cryo-ET to study the structural changes accompanying ...

As cryo-electron microscopy (cryo-EM) enters mainstream structural biology, the demand for fitting methods is high. Here, we review existing flexible fitting methods for cryo-EM. We discuss their importance, potential concerns and assessment strategies. We aim to give readers concrete descriptions of cryo-EM flexible fitting methods with corresponding examples.

Cryo-electron tomography (cryo-ET) has emerged as perhaps the only practical technique for revealing nanometer-level three-dimensional structural details of subcellular macromolecular complexes in their native context, inside the cell. As currently practiced, the specimen should be 0.1- 0.2 microns in thickness to achieve optimal resolution. Thus, application of cryo-ET to intact frozen (vitreo...

Cryogenic electron microscopy (cryo-EM) has extensively boosted structural biology research since the “resolution revolution” in year of 2013 which was soon awarded Nobel Prize Chemistry 2017. The advances camera techniques and software algorithms enabled cryo-EM to routinely characterize three-dimensional structures biomolecules at near-atomic resolution. Biomolecules are basically sensitive i...

Background: The effect of Dps-DNA co-crystals formation, which occurs in stressed Escherichia coli cells exposed to extreme conditions, is well described the literature. However, exact mechanisms formation are yet be postulated remaining largely unknown. Here we summarize results obtained by our group over last few years using cryo-Electron Microscopy (cryo-EM) and Small Angle X-ray Scattering ...

The production, via soft lithography, of micron-sized thermoresponsive pillars made of side-on nematic LCE leads to the formation of surface-responsive structures. The individual, monodisperse pillars, when cut out from the surface, behave as micro-actuators, showing contraction of around 35% at the nematic to isotropic phase transition.