General Lab Information

Qun Liu

Principal Investigator, Cellular Structural Biology, Biology Department

Qun Liu

Brookhaven National Laboratory

Biology Department
Bldg. 463, Room B136
P.O. Box 5000
Upton, NY 11973-5000

(631) 344-3417
(641) 403-6773
 qunliu@bnl.gov

Qun Liu obtained his Ph.D. in biophysics from Cornell University and did his postdoc research at Cornell Synchrotron Light Source (CHESS). After his postdoc training, he became a scientist at the New York Structural Biology Center; there he worked at the New York Consortium on Membrane Protein Structure as well as the X4 beamlines at the National Synchrotron Light Source (NSLS), Brookhaven National Laboratory. In 2015 Qun Liu joined the Biology Department of the Brookhaven National Laboratory as a Principle Investigator with a joint appointment from NSLS-II. Qun Liu is an Adjunct Professor and a faculty member of the Biochemistry and Structural Biology Program at Stony Brook University.

Research | Publications | Highlights

Research Activities

Membrane Protein Structural Biology: Membrane proteins form specialized gates connecting intracellular compartments and external environment, and are central for understanding information flux (for example, metabolites, nutrients, ions, and electrons) across membranes. Structural studies of these transmembrane gates and their functional characterizations may provide insights into understanding their roles in physiology and pathology. Our structural biology research focuses on the structures and mechanisms of membrane proteins and their complexes important in metal homeostasis, protein quality control, and metabolism.

Technology research and development: We are also interested in developing technologies that will enable or facilitate the membrane protein research. Different from soluble proteins, membrane proteins have hydrophobic transmembrane segments within and hydrophilic heads out of the lipid bilayer, respectively. Stabilization of membrane proteins for structural and functional characterization remains challenging. Eukaryotic membrane proteins are even more challenging owing to prevalent post-modifications and their different cellular localizations. To overcome these barriers, we are developing technologies by leveraging BNL capabilities of x-ray photon sciences at NSLS-II, LBMS Cryo-EM facility, nanotechnology and light microscopy at Center for Functional Nanomaterials (CFN), and data-driving discovery at Computational Science Initiative (CSI).

Selected Publications

  • Liu Q, Dahmane T, Zhang Z, et al (2012) Structures from Anomalous Diffraction of Native Biological Macromolecules. Science 336:1033–1037. https://doi.org/10.1126/science.1218753
  • Chang Y, Bruni R, Kloss B, et al (2014) Structural basis for a pH-sensitive calcium leak across membranes. Science 344:1131–1135. https://doi.org/10.1126/science.1252043
  • Liu Q (2017) TMBIM-mediated Ca2+ homeostasis and cell death. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1864:850–857. doi: 10.1016/j.bbamcr.2016.12.023
  • Guo G, Fuchs MR, Shi W, Skinner J, Berman E, Ogata CM, Hendrickson WA, McSweeney S, Liu Q (2018) Sample manipulation and data assembly for robust microcrystal synchrotron crystallography. IUCrJ 5:238–246. doi: 10.1107/s2052252518005389
  • Gao Y, Xu W, Shi W, Soares A, Jakoncic J, Myers S, Martins B, Skinner J, Liu Q, Bernstein H, McSweeney S, Nazaretski E, Fuchs MR (2018) High-speed raster-scanning synchrotron serial microcrystallography with a high-precision piezo-scanner. Journal of Synchrotron Radiation 25:1362–1370. doi: 10.1107/s1600577518010354
  • Guo G, Xu M, Chang Y, Luyten T, Seitaj B, Liu W, Zhu P, Bultynck G, Shi L, Quick M, Liu Q (2019) Ion and pH Sensitivity of a TMBIM Ca2+ Channel. Structure 27:1013–1021.e3. doi: 10.1016/j.str.2019.03.003
  • Guo G, Zhu P, Fuchs MR, Shi W, Andi B, Gao Y, Hendrickson WA, McSweeney S, Liu Q (2019) Synchrotron microcrystal native-SAD phasing at a low energy. IUCrJ 6:532–542. doi: 10.1107/s2052252519004536
  • Takemaru L, Guo G, Zhu P, Hendrickson WA, McSweeney S, Liu Q (2020) PyMDA: microcrystal data assembly using Python. Journal of Applied Crystallography 53:277–281. doi: 10.1107/s160057671901673x
  • Zhu P, Yu X-H, Wang C, Zhang Q, Liu W, McSweeney S, Shanklin J, Lam E, Liu Q (2020) Structural basis for Ca2+-dependent activation of a plant metacaspase. Nature Communications. doi: 10.1038/s41467-020-15830-8
  • McSweeney DM, McSweeney SM, Liu Q (2020) A self-supervised workflow for particle picking in cryo-EM. IUCrJ 7:719–727. doi: 10.1107/s2052252520007241
  • Chai J, Cai Y, Pang C, Wang L, McSweeney S, Shanklin J, Liu Q (2021) Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1. Nature Communications. doi: 10.1038/s41467-021-23533-x
  • Bruni R, Laguerre A, Kaminska A, et al (2021) High-throughput cell-free screening of eukaryotic membrane protein expression in lipidic mimetics. Protein Science 31:639–651. https://doi.org/10.1002/pro.4259
  • Chai L, Zhu P, Chai J, et al (2021) AlphaFold Protein Structure Database for Sequence-Independent Molecular Replacement. Crystals 11:1227. https://doi.org/10.3390/cryst11101227
  • Liu W, Schoonen M, Wang T, et al (2022) Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state. Communications Biology 5:. https://doi.org/10.1038/s42003-022-03213-2
  • Karasawa A, Andi B, Fuchs MR, et al (2022) Multi-crystal native-SAD phasing at 5 keV with a helium environment. IUCrJ 9:768–777. https://doi.org/10.1107/s205225252200971x
  • Dai X, Wu L, Yoo S, Liu Q (2023) Integrating AlphaFold and deep learning for atomistic interpretation of cryo-EM maps. https://doi.org/10.1101/2023.02.02.526877

Research Highlights

Qun Liu

Brookhaven National Laboratory

Biology Department
Bldg. 463, Room B136
P.O. Box 5000
Upton, NY 11973-5000

(631) 344-3417
(641) 403-6773
 qunliu@bnl.gov

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