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


Shashi Bhushan is an Assistant Professor at Nanyang Technological University of Singapore where he conducts research as a structural biologist employing single particle cryo-electron microscopy for research on biomolecular protein machinery. His research is focused on membrane protein and ribosomal complexes. Dr Bhushan has been an Editorial Board Member for Scientific Reports since 2017.




Wei-Hau Chang is an Associate Research Fellow at the Academia Sinica, Institute of Chemistry. His laboratory employs the-state-of-arts imaging methods to study the structure and dynamics of biological macromolecules. By developing streamlined computation methods, Dr Chang’s lab has generated many sub-3 Å cryo-EM structures of different sizes ranging from viruses to membrane proteins. Dr Chang has been an Editorial Board Member for Scientific Reports since 2019.




Christiane Riedel is a Scientist at the Vetmeduni in Vienna. She has a strong background in molecular virology and cryo electron tomography. Her research focus is the molecular and structural elucidation of pesti- and rhabdovirus entry and architecture. Dr Riedel has been an editorial board member for Scientific Reports since 2018.




Suparna Sanyal is a Professor of Molecular Biology at Uppsala University, Sweden. Her research focuses on solving molecular mechanisms of protein synthesis and protein folding by employing fast kinetics and structural biology (cryo-EM) using a fully reconstituted transcription-translation-folding (RTTF) system and covers the areas of antibiotic resistance and neurodegenerative diseases, exploring the role of ribosomal RNA. Her lab engineered the popular E. coli JE28 strain with His-tagged ribosomes. Prof Sanyal has been an Editorial Board Member for Scientific Reports since 2017.




Hans-Joachim Wieden is a Full Professor in the Department of Microbiology at the University of Manitoba, Canada and the Faculty of Science Lead for BioSciences Entrepreneurship and Industry Partnerships. His research focuses on the interface of the molecular structure, dynamics, and function of ribonucleoprotein complexes by integrating fast reaction kinetics and advocated biophysics with molecular dynamics simulation and structure determination. Prof Wieden has been an Editorial Board Member for Scientific Reports since 2015.



Nan Yao is the Founding Director of Princeton's Imaging and Analysis Center. His expertise is materials characterization for interdisciplinary research and applications, with a focus on the interface between physical and biological sciences. His publications include the co-discovery of the first natural quasicrystal, a finding that has revolutionized the science of natural crystal chemistry by identifying the third form of solid in nature besides crystalline and non-crystalline. Dr Yao has been an Editorial Board Member for Scientific Reports since 2013.