Proteins are involved in virtually every process within biological systems, and the function that a protein assumes depends on its structure. Determining the structure of a protein is of fundamental importance to understanding protein interactions, the role of proteins in diseases and disorders, drug design and more. Cryo-electron microscopy (cryo-EM) was developed as a cutting-edge alternative to X-ray crystallography, and alleviates the need for crystallization. With recent advances in electron detection and image processing, the resolution by cryo-EM is now beginning to rival X-ray crystallography. Our goal is to employ cryo-EM to determine high resolution structures of important membrane protein complexes involved in cellular signaling, including cellular receptors and ion channels. We also combine structural approaches with functional studies to reveal the structure-function relationships of these membrane proteins.

Structure Gallery
Four different RET signalling complexes
Cryo-EM structures of the extracellular region ternary complexes…
September 1, 2019/by Academic Web PagesInsulin receptor with four insulins bound
This is the first high resolution structure of IR-insulin complex…
September 2, 2019/by Academic Web PagesHuman mitochondrial calcium uniporter bound with EMRE
September 3, 2019/by Academic Web PagesThe proton channel OTOP3
The cryo-EM structure of OTOP3 from Xenopus tropicalis (XtOT…
September 4, 2019/by Academic Web PagesBai Lab
UT Southwestern Medical Center
5323 Harry Lines Boulevard
Dallas, TX 75390
Xiaochen.Bai@utsouthwestern.edu