Nobel laureate Dr. Joachim Frank discussed the history of molecular imaging and the process that led to his Nobel Prize as part of the Huck Distinguished Lecture Series on Wednesday evening in the Foster Auditorium.

Frank, a professor of biochemistry and molecular biophysics and biological sciences at Columbia University, was born in Germany in 1940. Frank earned his doctoral degree from the Technical University of Munich in 1970.

Frank worked on his research at the Max Planck Institute for Protein and Leather Research in Munich, Germany, the Cavendish Laboratory in Cambridge, England, and the Wadsworth Center in Albany, New York. 

For his work on image-processing techniques that proved essential to the development of cryo-electron microscopy (cryo-EM), Frank was awarded the Franklin Medal in Life Science in 2014, the Wiley Prize in Biomedical Sciences in 2017, and the Nobel Prize in Chemistry in 2017.

Frank began his lecture by speaking about the historical prospects and inventions that led to his revolutionary single-particle cryo-EM technique. The cryo-EM technique uses a flash-freezing system that stops the molecule but doesn’t kill the molecule by being so quick that ice doesn’t have a chance to form on the molecule.

The process of cryo-EM was brought about by the invention of the electron wave by Ernst Ruska in 1931. Unfortunately, the microscope couldn’t photograph biomolecules due to the nature of the electron wave.

“We have a saying in Germany that translates to ‘you shoot with cannons at sparrows,'” Frank said. “Because electrons impart so much energy and the molecule is just this very fragile thing, it is destroyed very quickly by the electron.”

This problem led to other developments in the field of biochemistry, like Robert Glaser’s discovery of just how sensitive biomolecules are to radiation later on in the 20th century.

Frank’s big breakthrough came in 1981 with the use of vitreous ice.

“Vitreous ice only forms with very fast plunging, and very fast heat transfer,” Frank said. “Because it is so fast, it does not kill the molecule.”

As one might expect, Frank’s process of molecular imaging is anything but simple. Single particle molecules must be flash frozen and photographed in under a millisecond. Molecules must be photographed numerous times before photos of the molecule in many different states are analyzed by a computer program that builds the 3D molecular structure being photographed.

Once a molecular structure is established, more pictures are taken using the newly structured molecule to find out how the molecule moves and interacts with other biomolecules around it. This type of research is currently being used to help learn more about E. coli and other bacteria.

Frank demonstrated the importance of experimental science versus prediction science. Through the rigorous amounts of photos taken using Frank’s method, he was able to disprove the predictions made by other scientists and form a more accurate 3D model of a molecule.

Frank said throughout his entire process of designing the new system, he always understood the importance of being thorough in his research.

“If there is no testing, there is no science,” Frank said. “We need experimental science in order to not mislead generations of future students. We need it now more than ever.”

The Huck Distinguished Lecture series wraps up its slate of spring semester speakers with University of British Columbia forest ecology professor Suzanne Simard at 4 p.m. on April 18 in the HUB’s Flex Theater.