Cryo-electron microscopy

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The first light microscope is thought to have been produced in the early 16th century. Of course it was much simpler than what is now available, however, as imaging technology has improved, resolution is no longer limited by the microscope, but by the wavelength of light itself; a different source of illumination is needed. Electron microscopes use a beam of electrons in place of light, and are therefore able to produce much higher resolution images. However, in order to visualise biomolecules directly (without burning them up), samples must be frozen and a gentler electron beam used: cryo-electron microscopy. Following a number of breakthroughs in the associated hardware and software over the last ten years, we have seen an explosion in the number of protein structures being determined by cryo-electron microscopy, and its application to studying larger structures – macromolecules, viruses, cells – has become much more widely mainstream.

This Collection invites original research presenting structures derived from cryo-EM as well as contributions to the underlying methods and technology.

Macrophage, TEM - stock photo


Collections articles undergo Scientific Reports' standard peer review process and are subject to all of the journal’s standard policies. This includes the journal’s policy on competing interests. The Guest Editors have no competing interests with the submissions which they handle through the peer review process. The peer review of any submissions for which the Guest Editors have competing interests is handled by another Editorial Board Member who has no competing interests.

This Collection has not been supported by sponsorship.