Microscopy Has Long Been Proven Fundamental?

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Microscopy has long been proven fundamental in structural biology, especially for the mechanistic understanding of virus cell architecture and macromolecular functions. Cryo-electron microscopy (cryo-EM) is a variation of electron microscopy that allows imaging of viruses in cryogenic solution (i.e. ethane solution cooled to near liquid nitrogen temperature) without having to grow crystals or embed samples in heavy metal salts (i.e. negative staining), using electrons to focus specimens with a resolution power to near-atomic details. Cryo-EM employs thin vitrified layers of unfixed, unstained and unsupported virus structures in cryogenic solutions (i.e. samples are preserved in or close to biological conditions) in easy controlled settings, yielding resolution powers to a near atomic resolution, affording this technique an overwhelming popularity in structural biology. Cryo-EM is now beginning to rival X-ray crystallography and NMR techniques to a near atomic details. This essay focuses on how cryo-EM have been implicated in visualizing virus structures with particular emphases on bacteriophage MS2 virion.

For a mechanistic understanding of macromolecular and biochemical functions and processes of a wide variety of biological structures (i.e. cells, proteins, bacteria and viruses) (Milne et al., 2013) optical devices (i.e. X-ray crystallography and NMR, among others) have long been implicated in characterizing biomolecular structures into 3D
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