K2 Summit camera used to solve Zika virus structure

Recently a team of researchers led by Purdue University unveiled the first three-dimensional structure of the Zika virus. Currently, this mosquito-borne virus is at the core of an epidemic in the Americas that has been linked to congenital microcephaly and Guillain-Barré syndrome. By using the K2 Summit^® camera, this groundbreaking achievement opens new opportunities for researchers to create antiviral treatments and vaccines for Zika and other know members of the Flavivirus genus.

Through single-particle cryo-electron microscopy (cryo-EM), researchers were able to solve mature Zika virus structure at near atomic resolution (3.8 Å), then compare it with other flavivirus structures (DOI: 10.1126/science.aaf5316). The K2 Summit camera from Gatan was the key detector used to determine the native virus structure.

The K2 Summit camera allowed researchers to identify differences in the region around the glycosylation site. When compared to previous published flavivirus structures and complexes, this region may modulate the sensitivity of Zika to antibodies, and be important for attachment to cellular lectin receptors.

According to the article released by Purdue University, Michael Rossmann, Purdue University’s Hanley Distinguished Professor of Biological Sciences, stated “We were able to determine through cryo-electron microscopy the virus structure at a resolution that previously would only have been possible through X-ray crystallography. Since the 1950s X-ray crystallography has been the standard method for determining the structure of viruses, but it requires a relatively large amount of virus, which isn’t always available; it can be very difficult to do, especially for viruses like Zika that have a lipid membrane and don’t organize accurately in a crystal; and it takes a long time. Now, we can do it through electron microscopy and view the virus in a more native state. This was unthinkable only a few years ago.”

This benchmark result further confirms that the K2 Summit camera is critical in solving in breakthrough cryo-EM structures. Not only is the K2 Summit defining the frontier of resolution for cryo-EM, but it is also being used to better understand virus transmission and disease maturation that are of worldwide concern.

About Cryo-EM

Cryo-EM is emerging as a major tool in a structural biologist’s arsenal, alongside conventional x-ray crystallography and NMR techniques, to study molecular interactions in supramolecular assemblies or biological machines.

Cryo-EM enables structure-based examination of native and hydrated biological complexes such as viruses, small organelles, and macromolecular biological complexes of 150 kDa or larger. Compared to conventional techniques, single-particle cryo-EM can provide resolutions approaching 2 Å for stable samples and allows you to obtain meaningful results with samples that are heterogeneous, metastable and extremely difficult to crystalize.

For more information regarding the K2 direct detection camera, please visit: http://www.gatan.com/K2