Tom Terwilliger teaches a course on Cryo-EM and Crystallography. The course was held on September 4-5, 2019 at the University of Buenos Aires, Argentina, and was titled Cryo-EM and Crystallography in the Forefront of Structural Biology. Tom Terwilliger is a Los Alamos National Laboratory scientist and New Mexico Consortium affiliate.
Cryo-electron microscopy (cryo-EM) is an emerging structural biology technique. In cryo-EM, the biological sample is prepared under cryogenic conditions. Cryo-EM is useful because it allows the observation of specimens that have not been stained or fixed in any way, showing them in the environment in which they were found. This differs from the usual method of X-ray crystallography. In X-ray crystallography, the specimen must be crystallized, which is a difficult process, and placed in non-physiological environments, which can lead to functional changes.
The resolution of cryo-EM maps is steadily improving. Near-atomic resolution of some structures have now been attained, including those of viruses, ribosomes, mitochondrial protein complexes, ion channels, and enzyme complexes. Researchers can use this method to calculate the structure of a biological macromolecule that has been flash-frozen in several conformations and thus can understand the mechanism by which it works.
During the September course, Terwilliger taught 32 students and postdocs from Argentina about the theory of X-ray crystallography and Cryo-electron microscopy. He also taught students how to use the Phenix software that he helped write to carry out both of these techniques.
Learning cryo-EM is important because the students will be the next generation of scientists figuring out the shapes of protein molecules such as proteins from human cells. This information can be used to design drugs that turn on or off these proteins and help control cancer and diseases.
Terwilliger is next teaching October 15-19, 2019 at Cold Springs Harbor Laboratory. He will be one of the speakers in a class on X-Ray Methods in Structural Biology. This course will teach participants extensive hands-on training in the lab on how to crystallize multiple proteins, and to determine their crystal structures through several methods.