When Mario Borgnia, Ph.D., heard that three scientists would share the 2017 Nobel Prize in Chemistry for developing cryo-electron microscopy (cryo-EM), he was ecstatic. As director of the new cryo-EM facility at NIEHS, his area of expertise was in the spotlight, and it was time to shine.
Cryo-EM lets scientists see the microscopic world via a special technique that quickly freezes a protein sample into a molecule-thin layer and uses an electron microscope to visualize the proteins in detail.
"Protein is the material that all living cells use to build their cellular machines and tools, so being able to see proteins in three dimensions is a big deal," Borgnia said. "Evolution shapes the structure of proteins to their particular function within a living organism."
Because a protein sample contains trillions of identical copies of the protein of interest, scientists use cryo-EM to see hundreds of them in a single field of view, with each protein appearing in a different orientation. Powerful computers then combine thousands of 2-D molecular images to construct a 3-D map of the protein. These detailed maps help structural biologists understand how these proteins work in healthy and diseased cells.
The NIEHS Cryo-EM Core opened June 2017 and is the first of its kind in North or South Carolina. Borgnia expects it to be a focal point for scientific exploration and a great way to work with researchers from across the Southeast.
The Molecular Microscopy Consortium
NIEHS is teaming up with Duke University and the University of North Carolina at Chapel Hill (UNC) to form the Molecular Microscopy Consortium. The consortium is a collaborative training environment that will build a strong cryo-EM presence in the region. While NIEHS is the first of the three institutions to have a functional cryo-EM facility, Duke and UNC expect to have their instruments operational in the near future.
To promote the use of cryo-EM, the consortium uses a dual strategy. First, it provides researchers with access to high-quality structural data using the latest instrumentation and methods.
That access is complemented with a focus on training scientists how to prepare specimens and process data. Trainees work and learn cryo-EM from members of the consortium, whose motto could be, “Do not send us a sample, rather, bring it with you and learn how to find your protein structure.”
Researchers who are not structural biologists and prefer not to learn cryo-EM are still invited to work with consortium staff on scientific projects. If you are a scientist interested in learning how to include cryo-EM in your studies, please contact Borgnia.