![]() ![]() ![]() Cryo-ET is generally restricted to investigations of small specimen volumes and the thin peripheral areas of cells (<500 nm) that are penetrable by the electron beam. Computationally extracted sub-tomograms can be averaged and classified to reveal sub-nanometer to nanometer resolution (3 Å to 4 nm) structures of in situ complexes 3, 4, 5. Cryo-electron tomography (cryo-ET) links three-dimensional (3D) contextual visualization and high-resolution structure determination of cryogenically preserved macromolecules in their native cellular environment 2. Cryo-electron microscopy (cryo-EM) of purified proteins (for example, single-particle cryo-EM) has propelled forward the cryo-EM ‘resolution revolution’ 1 resulting in an increasing interest in technologies to enable structure–function studies of macromolecules within the framework of larger biological systems. ![]()
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