Novel Protein Crystallization
Posted: Aug 31, 2022
James Moody is currently leading a novel protein crystallization project with the goal to make it faster and cheaper to determine the structures of proteins at the atomic scale. In order to see the structure of proteins at this level, he uses X-ray crystallography. Although very effective, this procedure is only useful for proteins that can be induced to form ordered crystals, making up only 10% of all known proteins. “Specifically, we aim to increase the speed and success rate of protein crystallization, which is required for protein X-ray crystallography,” said Moody.
Seeing the structure of proteins at the atomic level helps us to understand how protein dysfunction causes disease, which can lead to the development of new treatments and new protein-based tools.
Over the past year, the lab has been testing their protein crystallization technology called TELSAM against a large variety of proteins. TELSAM is a multivalent crystallization chaperone that can be described as a “helper protein” that helps another protein to crystallize more easily.
The students in Moody’s lab have had a very big role in this project. “Both graduate and undergraduate students carry out nearly every step of the process,” says Moody. “They design the new proteins to be tested, assemble the DNA and reprogram the bacteria, produce and purify the protein, set up the crystallization experiments, collect the X-ray diffraction data, and solve the atomic level protein structures.”
Moody and his students are currently working on designing and testing new versions of TELSAM that will work better and for a larger set of protein targets.