Electron cryo-microscopy (cryo-EM) single-particle analysis has yielded protein structures with increasing levels of detail in recent years1,2. However, it has proved difficult to obtain cryo-EM reconstructions with sufficient resolution to visualize individual atoms in proteins. Here we use a new ...
we wanted to explore whether STEM imaging can be applied to vitrified biological samples and produce high-resolution images. Using iDPC–STEM imaging of KLH, we here report the successful subnanometer single-particle cryo-EM structure at 6.5 Å resolution. More systematically, using iDPC–STEM...
Since cytoskeletal polymers are difficult to crystallize, cryo-EM has been the predominant method of choice to study their structures. Recent advances in the methodology have enabled reconstructions at near-atomic resolution. In this review, we focus on novel insights gained from high-resolution cryo...
Single particle cryo em is a powerful structural biology technique for 3D characterization of proteins, protein complexes and macromolecules at near-atomic and atomic resolution.
Single particle cryo em is a powerful structural biology technique for 3D characterization of proteins, protein complexes and macromolecules at near-atomic and atomic resolution.
Single particle cryo em is a powerful structural biology technique for 3D characterization of proteins, protein complexes and macromolecules at near-atomic and atomic resolution.
The power of single-particle cryo-EM should make it possible to determine the structure of an intact carboxysome at near-atomic resolution. However, there remains multiple practical challenges for this.61 Because of the structural heterogeneity mentioned above, a very large number of particles will ...
Single particle cryo em is a powerful structural biology technique for 3D characterization of proteins, protein complexes and macromolecules at near-atomic and atomic resolution.
In the recent years, the protein databank has been fueled by the exponential growth of high-resolution electron cryo-microscopy (cryo-EM) structures. This trend will be further accelerated through the continuous software and method developments and the i
In this work, we have used single-particle cryo-electron microscopy to determine the structure of prestin from gerbil (Meriones unguiculatus) at subnanometer resolution that confirms Oliver’s initial modeling efforts25and, remarkably, bears high concordance with the recently determined cryo-EM structures...