Fan Lab focuses on interdisciplinary approaches, leveraging technical strengths to develop novel cryo-EM imaging technologies, as well as efficient sample preparation and data processing methods. The group aims to establish a platform for in situ structural and functional analysis of membrane proteins within native membrane systems. Utilizing this platform, the group will conduct high-efficiency in situ studies of complex biomembrane environments, analyzing the spatial conformations, interaction networks, and multiscale organizational patterns of key macromolecules. This work will explore the coupling and regulatory mechanisms between biomembrane systems, providing a theoretical foundation for disease intervention.

Dr. Fan has long been dedicated to integrating cutting-edge multidisciplinary techniques to advance cryo-electron microscopy (cryo-EM) technology innovation, focusing on structural biology research related to the interaction mechanisms of membrane proteins and drug molecules in major diseases. By developing a comprehensive cryo-EM technology system, Dr. Fan has overcome longstanding technical bottlenecks in the field, successfully achieving high-resolution structural analysis of small proteins and membrane proteins in near-physiological states. These efforts have led to a series of significant discoveries, including elucidating the structure and pharmacological mechanisms of voltage-gated sodium/calcium ion channels.

Human Frontier Science Program (HFSP) Postdoctoral Fellowship Award

* Equal contributions # Corresponding author

[1] Lu, F.*, Huang, X.*, Cai, G.*, Shen, X., Xie, Y., Huang, P., Yu, F., Fan, X.# and Huang, J.#, Structural basis for the assembly and modulation of human M-channels. Vita 2026. https://doi.org/10.15302/vita.2026.05.0035

[2] Fan, X.*, Huang, J.*#, Yang, L.*, Chen, J., Wang, H., Huang, X., Geng, J., Wu, Q., Xie, Y., Lu, F., Guo, Q., Shen, Z., Jin, X.# and Yan, N.#. Diverse binding poses of agonistic neurotoxins on human Nav1. 6. Nature 2026, pp.1-10. https://doi.org/10.1038/s41586-026-10661-x

[3] Fan, X.*#, Chen, J.*, Xue, L.*, Wang, H., Wu, T., Huang, X., Lu, F., Jin, X., Song, C., Huang, J.# and Yan, N.#. Open-state structure of veratridine-activated human Nav1. 7 reveals the molecular choreography of fast inactivation. Vita 2026, 1(1): 19-31. https://doi.org/10.15302/vita.2026.01.0003

[4] Fan, X.*, Chen, J*., Huang, X., Hou, Z., Xie, Y., Li, Z., Yan, N.# and Huang, J.#. Phrixotoxin-3 binds to three distinct antagonistic sites on human Nav1. 6. Cell Research 2025, 35(8): 610-613.

[5] Yang, Z.*, Fan, X.* and Wang, H.W.#. Near-atomic resolution single-particle 3D reconstruction using a single Cryo-EM micrograph. Journal of Chinese Electron Microscopy Society 2025, 44 (1): 1000-6281.

[6] Huang, J.*, Fan, X.*#, Jin, X., Lyu, C., Guo, Q., Liu, T., Chen, J., Davakan, A., Lory, P. and Yan, N.#. Structural basis for human Cav3. 2 inhibition by selective antagonists. Cell Research 2024, 34(6): 440-450.

[7] Yang, Z., Fan, J., Wang, J., Fan, X., Ouyang, Z., Wang, H.W.# and Zhou, X.#. Electrospray-assisted cryo-EM sample preparation to mitigate interfacial effects. Nature Methods 2024, 21(6): 1023-1032.

[8] Fan, X. *#, Huang, J.*, Jin, X. and Yan, N.#. Cryo-EM structure of human voltage-gated sodium channel Nav1. 6. Proceedings of the National Academy of Sciences 2023, 120(5): p.e2220578120.

[9] Huang, J.*, Fan, X.*#, Jin, X., Teng, L. and Yan, N.#, 2023. Dual-pocket inhibition of Nav channels by the antiepileptic drug lamotrigine. Proceedings of the National Academy of Sciences 2023, 120(41): p.e2309773120.

[10] Wu, Q.*, Huang, J.*#, Fan, X.*#, Wang, K.*, Jin, X., Huang, G., Li, J., Pan, X.# and Yan, N.#. Structural mapping of Nav1. 7 antagonists. Nature communications 2023, 14(1): 3224.

[11] Huang, J.*, Fan, X.*, Jin, X., Jo, S., Zhang, H.B., Fujita, A., Bean, B.P.# and Yan, N.#. Cannabidiol inhibits Nav channels through two distinct binding sites. Nature communications 2023, 14(1): 3613.

[12] Shen, J.*, Hu, M.*, Fan, X.*#, Ren, Z., Portioli, C., Yan, X., Rong, M. and Zhou, M.#. Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport. Structure 2022, 30(7): 1035-1041.

[13] Ni, H.*, Fan, X.*, Zhou, F., Guo, G., Lee, J.Y., Seeman, N.C., Kim, D.N., Yao, N., Chaikin, P.M. and Han, Y.#. Direct visualization of floppy two-dimensional DNA origami using cryogenic electron microscopy. iScience 2022, 6(25): 104373.

[14] Yao, X.*, Fan, X.*# and Yan, N.#. Cryo-EM analysis of a membrane protein embedded in the liposome. Proceedings of the National Academy of Sciences 2020, 117(31): 18497-18503.

[15] Han, Y.*, Fan, X.*, Wang, H., Zhao, F., Tully, C.G., Kong, J., Yao, N. and Yan, N.#. High-yield monolayer graphene grids for near-atomic resolution cryoelectron microscopy. Proceedings of the National Academy of Sciences 2020, 117(2): 1009-1014.

[16] Fan, X.*, Wang, J.*, Zhang, X., Yang, Z., Zhang, J.C., Zhao, L., Peng, H.L., Lei, J. and Wang, H.W., 2019. Single particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution. Nature Communications 2019, 10(1): 2386.

[17] Wang, H.W. and Fan, X. Challenges and opportunities in cryo-EM with phase plate. Current Opinion in Structural Biology 2019, 58: 175-182.

[18] Fan, X.*, Zhao, L.*, Liu, C., Zhang, J.C., Fan, K., Yan, X., Peng, H.L., Lei, J.# and Wang, H.W.#. Near-atomic resolution structure determination in over-focus with volta phase plate by Cs-corrected cryo-EM. Structure 2017, 25(10):1623-1630.

Our group is currently recruiting Associate Researchers / Assistant Researchers and Postdoctoral Fellows.