I earned my master’s degree from Tsinghua University in China. I worked in the laboratory of Dr. Yigong Shi, where I combined structural (X-ray crystallography) and biophysical assays to study bacterial transporter and channel proteins. Fascinated by the intertwined roles played by molecular structure and conformational dynamics in determining the functional mechanisms of integral membrane proteins, I became interested in single-molecule biophysics and other cutting-edge methodologies that can probe the dynamics of receptor proteins. I did my Ph.D. work with Dr. John Kuriyan at UC Berkeley. I opened up a new research direction in the lab by applying single-molecular fluorescence microscopy and spectroscopy to study the spatial and temporal regulation of EGF receptor (EGFR) on live cell membranes. Near the end of my Ph.D., I made significant breakthroughs in developing a mammalian cell-based expression and purification system that would allow me to pursue the longsought structural studies of full-length human EGFR using cryo-EM. As an HHMI postdoctoral fellow in the Kuriyan lab, I developed a suite of strategies to successfully reconstitute EGFR into membrane mimetics. After years of efforts, I recently reported the results of the first cryo-EM analysis of full-length human EGFR bound to two ligands, EGF and TGF-a, which provided significant insights into how these receptors work at the molecular level and uncovered the importance of conformational dynamics in regulating RTKs function.