cryoelectron microscopies การใช้

X-ray diffraction and cryoelectron microscopy suggest that tropomyosin sterically blocks the access of myosin to the actin filament.
This paper is generally considered to mark the origin of cryoelectron microscopy, and the technique has been developed to the point of becoming routine at several laboratories throughout the world.
The utility of cryoelectron microscopy stems from the fact that it allows the observation of specimens that have not been stained or fixed in any way, showing them in their native environment.
However, recent investigation provides an alternative structure of 19S base via an integrative approach combining data from cryoelectron microscopy, X-ray crystallography, residue-specific chemical cross-linking, and several proteomics techniques.
A more recent expansion applies the spatial-restraint model to electron density maps derived from cryoelectron microscopy studies, which provide low-resolution information that is not usually itself sufficient to generate atomic-resolution structural models.