Academic

Within the past five years, breakthrough of resolution in single-particle cryo-electron microscopy (cryo-EM) has transformed it into a main-stream tool for high-resolution protein structure determination. In contrast to X-ray crystallography, cryo-EM has the advantage of avoiding crystallization in preparing the particle sample. However, this advantage in sample preparation results in a challenge in image analysis that the particle orientation information is missed. Additionally, to minimize the radiation damage on biological particles, very low dose of electron beam is applied to extract the particle density information, which leads to extremely low signal to noise ratio data. In this talk, I will introduce some challenging problems, present our studies and demonstrate its performance on some benchmark datasets.