Center for Biomolecular and Cellular Structure
(Protein Communication Group)

Since the structure of myoglobin was first determined in the 1950s by X-ray crystallography, this technique has been the most powerful tool in modern structural biology. Recently, a resolution revolution in single particle Cryo-EM has been led by technical breakthroughs, particularly direct electron detector (DED) with unprecedented speed and sensitivity, a state of the art electron microscope (Titan Krios), image processing software with better algorithms and GPG-based parallel computation. The great advantage of Cryo-EM is that it can determine the 3D structure of macromolecular complexes in near native condition with a much smaller amount of sample, and can even capture multiple dynamic states by using advanced image-processing algorithms. These achievements herald the beginning of a new era in the field of structural biology and has been appreciated as the Method of the Year 2015 by Nature Methods and the Nobel prizes in chemistry, 2017.

Our research group is undertaking innovative research to discover the novel binding targets of uncharacterized LRR-containing proteins and their cellular signaling network. These novel binding partners for uncharacterized LRR-containing proteins as well as the supramolecular signaling complexes will be the key targets for our structural research. To this end, our research group would like to establish four core facilities (Protein Expression core, high-performance Cryo-EM core, Protein Crystallization core, and Computing core for Cryo-EM image processing) at IBS Headquarter. Our challenging approach will contribute to understand the molecular mechanism of uncharacterized LRR-containing proteins as well as their physiological and pathological roles. We also hope that the upcoming Core-facility at the IBS Headquarter promote internal/external collaborations ranging from design and analysis of various macromolecular complexes.