Principal Investigators
Principal Investigators
en Research Principal Investigators
Long Gui

Principal Investigator

Research Area

Structural Biology

Email

guilong(at)smart.org.cn

Research Interests

Cryo-Electron Tomography, In-situ Structural Biology, Structural Biology, Cell Biology, Virology.


Founded in 2024 at Shenzhen Medical Academy of Research and Translation, the Gui Lab specializes in revealing the structure and interactions of cellular macrocomplexes in their native context. Our approach combines cutting-edge methods like cryo-electron tomography, cryo-focused ion beam milling, high-pressure freezing, and correlative light and electron microscopy. Our research encompasses a broad range of biological specimens including organelles, intact cells, and tissues, with special emphasis on 


1) the virus-cell and cell-cell membrane fusion; 


2) the architecture of the primary cilia in mammalian cells; and 


3) the interactions between immune and cancer cells.

Education & Work Experience

2024 - PresentJunior Principal Investigator, Shenzhen Medical Academy of Research and Translation

2017 - 2023Postdoctoral Research Fellow, University of Texas Southwestern Medical Center

2016 - 2017Postdoctoral Research Fellow, University of Washington

2009 - 2016Ph.D. in Medicinal Chemistry (Biological Physics, Structure and Design Graduate Program), University of Washington

2005 - 2009Bachelor of Science, University of Science and Technology of China

Awards & Honors

2013     Margaret R. Davis Endowed Graduate Student Award 

2008     Outstanding Undergraduate Scholarship (Grade 2 for top 10%)

2007     Outstanding Undergraduate Scholarship (Grade 1 for top 3%) 

2006     Guanghua Education Scholarship 

2005     Outstanding Undergraduate Scholarship (Grade 3 for top 20%) 

Representative Publications

* for co-author.


1.Gui, L., O’Shaughnessy, W.J., Cai, K., Reetz, E., Reese, M.L. and Nicastro, D., 2023. Cryo-electron tomography of the apicomplexan invasion machinery in its native state reveals rigid body motion of the conoid and docked secretory machinery. Nature Communications, 14(1):1775.


2.Rogers, S.*, Gui, L.*, Kovalenko, A.*, Zoni, V.*, Carpentier, M., Ramji, K., Ben Mbarek, K., Bacle, A., Fuchs, P., Campomanes, P. and Reetz, E., 2022. Triglyceride lipolysis triggers liquid crystalline phases in lipid droplets and alters the LD proteome. Journal of Cell Biology221(11), p.e202205053.


3.Pinskey, J.M., Lagisetty, A., Gui, L., Phan, N., Reetz, E., Tavakoli, A., Fu, G. and Nicastro, D., 2022. Three-dimensional flagella structures from animals’ closest unicellular relatives, the Choanoflagellates. Elife11, p.e78133.


4.Gui, L., Song, K., Tritschler, D., Bower, R., Yan, S., Dai, A., Augspurger, K., Sakizadeh, J., Grzemska, M., Ni, T. and Porter, M.E., 2019. Scaffold subunits support associated subunit assembly in the Chlamydomonas ciliary nexin–dynein regulatory complex. Proceedings of the National Academy of Sciences116(46), pp.23152-23162.


5.Stoddard, D., Zhao, Y., Bayless, B.A., Gui, L., Louka, P., Dave, D., Suryawanshi, S., Tomasi, R.F.X., Dupuis-Williams, P., Baroud, C.N. and Gaertig, J., 2018. Tetrahymena RIB72A and RIB72B are microtubule inner proteins in the ciliary doublet microtubules. Molecular Biology of the Cell29(21), pp.2566-2577.


6.Gui, L. and Lee, K.K., 2018. Influenza virus-liposome fusion studies using fluorescence dequenching and cryo-electron tomography. Influenza Virus: Methods and Protocols, pp.261-279.


7.Gui, L., Ebner, J.L., Mileant, A., Williams, J.A. and Lee, K.K., 2016. Visualization and sequencing of membrane remodeling leading to influenza virus fusion. Journal of virology90(15), pp.6948-6962.


8.Gui, L., Jurgens, E.M., Ebner, J.L., Porotto, M., Moscona, A. and Lee, K.K., 2015. Electron tomography imaging of surface glycoproteins on human parainfluenza virus 3: association of receptor binding and fusion proteins before receptor engagement. MBio6(1), pp.10-1128.


9.He, Y.X., Gui, L., Liu, Y.Z., Du, Y., Zhou, Y., Li, P. and Zhou, C.Z., 2009. Crystal structure of Saccharomyces cerevisiae glutamine synthetase Gln1 suggests a nanotube‐like supramolecular assembly. Proteins: Structure, Function, and Bioinformatics76(1), pp.249-254.