Department of Structural Biology

The Department of Structural Biology aims to understand biology and human diseases at their most basic level. Scientists in the department use a series of advanced biophysical and biochemical techniques, such as cryo-electron microscopy, X-ray crystallography, mass spectrometry and patch-clamp electrophysiology, to determine the atomic structures of proteins and protein-nucleic acid complexes and investigate their biological functions both in vitro with purified samples and in cells. The determination of these structures illuminates the underpinnings of normal cellular function as well as disease-related dysfunction. They also reveal the action mechanisms of many existing drugs and may guide the development of novel therapeutics.


Recent Publications

Ruan Z*, Haley E*, Orozco I*, Sabat M, Myers R, Roth R, Du J#, Lü W#. 2021. Structures of the TRPM5 channel elucidate mechanisms of activation and inhibition. Nat Struct Mol Biol.

Xu T-H, Liu M, Zhou XE, Liang G, Zhao G, Xu HE#, Melcher K#, Jones PA# 2020. Structure of DNA methyltransferases DNMT3A/DNMT3B bound to a nucleosomeNature 586:151–155.
#Co-corresponding authors

Bai L, You Q, Jain BK, Duan HD, Kovach A, Graham TR, Li H. 2020. Transport mechanism of P4 ATPase phosphatidylcholine flippases. eLife. 

Zhou Y, Zhou XE, Gong Y, Zhu Y, Cao X, Brunzelle JS, Xu HE, Zhou M, Melcher K#, Zhang F#. 2020. Structural basis of Fusarium myosin I inhibition by phenemacril. PLOS Pathog.
# Co-corresponding authors

Ruan Z*, Osei-Owusu J*, Du J, Qiu Z#, Lü W#. 2020. Structures and pH-sensing mechanism of the proton-activated chloride channel. Nature.

Bai L, You Q, Feng X, Kovach A, Li H. 2020. Structure of the ER membrane complex, a transmembrane-domain insertase. Nature.