Representative Publications with data obtained at the facility
Year 2025
Bi, M., Wang, X., Wang, J., Xu, J., Sun, W., Adediwura, V. A., Miao, Y., Cheng, Y., & Ye, L. (2025). Structure and function of a near fully-activated intermediate GPCR-Gαβγ complex. Nature Communications, 16(1), 1100. https://doi.org/10.1038/s41467-025-56434-4
Koide, E., Pietz, H. L., Beltran, J., & Chen, J. (2025). Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2. Nature Communications, 16(1), 484. https://doi.org/10.1038/s41467-024-55810-w
Zhou, H., Huertas, J., Julia Maristany, M., Russell, K., Hwang, J. H., Yao, R.-W., Hutchings, J., Shiozaki, M., Zhao, X., Doolittle, L. K., Gibson, B. A., Riggi, M., Espinosa, J. R., Yu, Z., Villa, E., Collepardo-Guevara, R., & Rosen, M. K. (2025). Multi-scale structure of chromatin condensates rationalizes phase separation and material properties. In bioRxiv (p. 2025.01.17.633609). https://doi.org/10.1101/2025.01.17.633609
Year 2024
Barrero, D. J., Wijeratne, S. S., Zhao, X., Cunningham, G. F., Yan, R., Nelson, C. R., Arimura, Y., Funabiki, H., Asbury, C. L., Yu, Z., Subramanian, R., & Biggins, S. (2024). Architecture of native kinetochores revealed by structural studies utilizing a thermophilic yeast. Current Biology : CB, 34(17), 3881–3893.e5. https://doi.org/10.1016/j.cub.2024.07.036
Borowska, M. T., Liu, L. D., Caveney, N. A., Jude, K. M., Kim, W.-J., Masubuchi, T., Hui, E., Majzner, R. G., & Garcia, K. C. (2024). Orientation-dependent CD45 inhibition with viral and engineered ligands. Science Immunology, 9(100), eadp0707. https://doi.org/10.1126/sciimmunol.adp0707
Cao, S., Garcia, S. F., Shi, H., James, E. I., Kito, Y., Shi, H., Mao, H., Kaisari, S., Rona, G., Deng, S., Goldberg, H. V., Ponce, J., Ueberheide, B., Lignitto, L., Guttman, M., Pagano, M., & Zheng, N. (2024). Recognition of BACH1 quaternary structure degrons by two F-box proteins under oxidative stress. Cell, 187(26), 7568–7584.e22. https://doi.org/10.1016/j.cell.2024.10.012
Clark, S., Jeong, H., Posert, R., Goehring, A., & Gouaux, E. (2024). The structure of the Caenorhabditis elegans TMC-2 complex suggests roles of lipid-mediated subunit contacts in mechanosensory transduction. Proceedings of the National Academy of Sciences of the United States of America, 121(8), e2314096121. https://doi.org/10.1073/pnas.2314096121
Du, H., Liu, J., Jude, K. M., Yang, X., Li, Y., Bell, B., Yang, H., Kassardjian, A., Blackson, W., Mobedi, A., Parekh, U., Parra Sperberg, R. A., Julien, J.-P., Mellins, E. D., Garcia, K. C., & Huang, P.-S. (2024). A general system for targeting MHC class II-antigen complex via a single adaptable loop. Nature Biotechnology. https://doi.org/10.1038/s41587-024-02466-y
Eisenberg, D., Hou, K., Ge, P., Sawaya, M., Dolinsky, J., Yang, Y., Jiang, Y. X., Lutter, L., Boyer, D., Cheng, X., Pi, J., Zhang, J., Lu, J., Yang, S., Yu, Z., & Feigon, J. (2024). How short peptides can disassemble ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism. In Res Sq. https://doi.org/10.21203/rs.3.rs-4152095/v1
Fu, Z., & MacKinnon, R. (2024). Structure of the flotillin complex in a native membrane environment. Proceedings of the National Academy of Sciences of the United States of America, 121(29), e2409334121. https://doi.org/10.1073/pnas.2409334121
Gan, N., Zeng, W., Han, Y., Chen, Q., & Jiang, Y. (2024). Structural mechanism of proton conduction in otopetrin proton channel. Nature Communications, 15(1), 7250. https://doi.org/10.1038/s41467-024-51803-x
Lee, J., Oldham, M. L., Manon, V., & Chen, J. (2024). Principles of peptide selection by the transporter associated with antigen processing. Proceedings of the National Academy of Sciences of the United States of America, 121(23), e2320879121. https://doi.org/10.1073/pnas.2320879121
Leng, F., Merino, R., Wang, X., Zhang, W., Ha, T., & Hur, S. (2024). Ultrastable and Versatile FoxP3 Ensembles on Microsatellites. In bioRxiv (p. 2024.12.12.628245). https://doi.org/10.1101/2024.12.12.628245
Matsui, A., Spangler, C., Elferich, J., Shiozaki, M., Jean, N., Zhao, X., Qin, M., Zhong, H., Yu, Z., & Gouaux, E. (2024). Cryo-electron tomographic investigation of native hippocampal glutamatergic synapses. eLife, 13. https://doi.org/10.7554/eLife.98458
Rickgauer, J. P., Choi, H., Moore, A. S., Denk, W., & Lippincott-Schwartz, J. (2024). Structural dynamics of human ribosomes in situ reconstructed by exhaustive high-resolution template matching. Molecular Cell, 84(24), 4912–4928.e7. https://doi.org/10.1016/j.molcel.2024.11.003
Srivastava, D. K., Navratna, V., Tosh, D. K., Chinn, A., Sk, M. F., Tajkhorshid, E., Jacobson, K. A., & Gouaux, E. (2024). Structure of the human dopamine transporter and mechanisms of inhibition. Nature, 632(8025), 672–677. https://doi.org/10.1038/s41586-024-07739-9
Wang, N., Waghray, D., Caveney, N. A., Jude, K. M., & Garcia, K. C. (2024). Structural insights into human MHC-II association with invariant chain. Proceedings of the National Academy of Sciences of the United States of America, 121(19), e2403031121. https://doi.org/10.1073/pnas.2403031121
Zhao, J., Chen, A. Q., Ryu, J., & Del Mármol, J. (2024). Structural basis of odor sensing by insect heteromeric odorant receptors. Science (New York, N.Y.), 384(6703), 1460–1467. https://doi.org/10.1126/science.adn6384
Zhao, X. (2024). Unlocking cryo-EM’s multishot potential with square or rectangular beams. Nature Methods, 21(4), 555–557. https://doi.org/10.1038/s41592-024-02224-7
Zhou, H., Hutchings, J., Shiozaki, M., Zhao, X., Doolittle, L. K., Yang, S., Yan, R., Jean, N., Riggi, M., Yu, Z., Villa, E., & Rosen, M. K. (2024). Quantitative Spatial Analysis of Chromatin Biomolecular Condensates using Cryo-Electron Tomography. In bioRxiv. https://doi.org/10.1101/2024.12.01.626131
Year 2023
Alexander, J. A. N., Worrall, L. J., Hu, J., Vuckovic, M., Satishkumar, N., Poon, R., Sobhanifar, S., Rosell, F. I., Jenkins, J., Chiang, D., Mosimann, W. A., Chambers, H. F., Paetzel, M., Chatterjee, S. S., & Strynadka, N. C. J. (2023). Structural basis of broad-spectrum β-lactam resistance in Staphylococcus aureus. Nature, 613(7943), 375–382. https://doi.org/10.1038/s41586-022-05583-3
Chen, Z., Greenan, G. A., Shiozaki, M., Liu, Y., Skinner, W. M., Zhao, X., Zhao, S., Yan, R., Yu, Z., Lishko, P. V., Agard, D. A., & Vale, R. D. (2023). In situ cryo-electron tomography reveals the asymmetric architecture of mammalian sperm axonemes. Nature Structural & Molecular Biology, 30(3), 360–369. https://doi.org/10.1038/s41594-022-00861-0
Chen, Z., Shiozaki, M., Haas, K. M., Skinner, W. M., Zhao, S., Guo, C., Polacco, B. J., Yu, Z., Krogan, N. J., Lishko, P. V., Kaake, R. M., Vale, R. D., & Agard, D. A. (2023). De novo protein identification in mammalian sperm using in situ cryoelectron tomography and AlphaFold2 docking. Cell, 186(23), 5041–5053.e19. https://doi.org/10.1016/j.cell.2023.09.017
Falzone, M. E., & MacKinnon, R. (2023a). Gβγ activates PIP2 hydrolysis by recruiting and orienting PLCβ on the membrane surface. Proceedings of the National Academy of Sciences of the United States of America, 120(20), e2301121120. https://doi.org/10.1073/pnas.2301121120
Falzone, M. E., & MacKinnon, R. (2023b). The mechanism of Gαq regulation of PLCβ3-catalyzed PIP2 hydrolysis. Proceedings of the National Academy of Sciences of the United States of America, 120(48), e2315011120. https://doi.org/10.1073/pnas.2315011120
Feng, S., Puchades, C., Ko, J., Wu, H., Chen, Y., Figueroa, E. E., Gu, S., Han, T. W., Ho, B., Cheng, T., Li, J., Shoichet, B., Jan, Y. N., Cheng, Y., & Jan, L. Y. (2023). Identification of a drug binding pocket in TMEM16F calcium-activated ion channel and lipid scramblase. Nature Communications, 14(1), 4874. https://doi.org/10.1038/s41467-023-40410-x
Kaplan, M., Chang, Y.-W., Oikonomou, C. M., Nicolas, W. J., Jewett, A. I., Kreida, S., Dutka, P., Rettberg, L. A., Maggi, S., & Jensen, G. J. (2023). Bdellovibrio predation cycle characterized at nanometre-scale resolution with cryo-electron tomography. Nature Microbiology, 8(7), 1267–1279. https://doi.org/10.1038/s41564-023-01401-2
Lucas, B. A., & Grigorieff, N. (2023). Quantification of gallium cryo-FIB milling damage in biological lamellae. Proceedings of the National Academy of Sciences of the United States of America, 120(23), e2301852120. https://doi.org/10.1073/pnas.2301852120
Mandala, V. S., & MacKinnon, R. (2023). The membrane electric field regulates the PIP2-binding site to gate the KCNQ1 channel. Proceedings of the National Academy of Sciences, 120(21), e2301985120. https://doi.org/10.1073/pnas.2301985120
Miller, A. N., Houlihan, P. R., Matamala, E., Cabezas-Bratesco, D., Lee, G. Y., Cristofori-Armstrong, B., Dilan, T. L., Sanchez-Martinez, S., Matthies, D., Yan, R., Yu, Z., Ren, D., Brauchi, S. E., & Clapham, D. E. (2023). The SARS-CoV-2 accessory protein Orf3a is not an ion channel, but does interact with trafficking proteins. eLife 12:e84477. https://doi.org/10.7554/eLife.84477
Nguyen, C., Lei, H.-T., Lai, L. T. F., Gallenito, M. J., Mu, X., Matthies, D., & Gonen, T. (2023). Lipid flipping in the omega-3 fatty-acid transporter. Nature Communications, 14(1), 2571. https://doi.org/10.1038/s41467-023-37702-7
Song, J., Gooding, A. R., Hemphill, W. O., Love, B. D., Robertson, A., Yao, L., Zon, L. I., North, T. E., Kasinath, V., & Cech, T. R. (2023). Structural basis for inactivation of PRC2 by G-quadruplex RNA. Science (New York, N.Y.), 381(6664), 1331–1337. https://doi.org/10.1126/science.adh0059
Sun, C., Zhu, H., Clark, S., & Gouaux, E. (2023). Cryo-EM structures reveal native GABAA receptor assemblies and pharmacology. Nature, 622(7981), 195–201. https://doi.org/10.1038/s41586-023-06556-w
Tao, X., Zhao, C., & MacKinnon, R. (2023). Membrane protein isolation and structure determination in cell-derived membrane vesicles. Proceedings of the National Academy of Sciences of the United States of America, 120(18), e2302325120. https://doi.org/10.1073/pnas.2302325120
Tsutsumi, N., Masoumi, Z., James, S. C., Tucker, J. A., Winkelmann, H., Grey, W., Picton, L. K., Moss, L., Wilson, S. C., Caveney, N. A., Jude, K. M., Gati, C., Piehler, J., Hitchcock, I. S., & Garcia, K. C. (2023). Structure of the thrombopoietin-MPL receptor complex is a blueprint for biasing hematopoiesis. Cell, 186(19), 4189–4203.e22. https://doi.org/10.1016/j.cell.2023.07.037
Wang, W., Götte, B., Guo, R., & Pyle, A. M. (2023). The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization. Nature Communications, 14(1), 7308. https://doi.org/10.1038/s41467-023-42982-0
Wright, K. M., DiNapoli, S. R., Miller, M. S., Aitana Azurmendi, P., Zhao, X., Yu, Z., Chakrabarti, M., Shi, W., Douglass, J., Hwang, M. S., Hsiue, E. H.-C., Mog, B. J., Pearlman, A. H., Paul, S., Konig, M. F., Pardoll, D. M., Bettegowda, C., Papadopoulos, N., Kinzler, K. W., Vogelstein, B., Zhou, S., & Gabelli, S. B. (2023). Hydrophobic interactions dominate the recognition of a KRAS G12V neoantigen. Nature Communications, 14(1), 5063. https://doi.org/10.1038/s41467-023-40821-w
Xu, L., Liu, T., Chung, K., & Pyle, A. M. (2023). Structural insights into intron catalysis and dynamics during splicing. Nature, 624(7992), 682–688. https://doi.org/10.1038/s41586-023-06746-6
Yang, D., Zhao, Z., Tajkhorshid, E., & Gouaux, E. (2023). Structures and membrane interactions of native serotonin transporter in complexes with psychostimulants. Proceedings of the National Academy of Sciences of the United States of America, 120(29), e2304602120. https://doi.org/10.1073/pnas.2304602120
Zhang, J., Zeng, W., Han, Y., Lee, W.-R., Liou, J., & Jiang, Y. (2023). Lysosomal LAMP proteins regulate lysosomal pH by direct inhibition of the TMEM175 channel. Molecular Cell, 83(14), 2524–2539.e7. https://doi.org/10.1016/j.molcel.2023.06.004
Zhang, W., Leng, F., Wang, X., Ramirez, R. N., Park, J., Benoist, C., & Hur, S. (2023). FOXP3 recognizes microsatellites and bridges DNA through multimerization. Nature, 624(7991), 433–441. https://doi.org/10.1038/s41586-023-06793-z
Year 2022
Cai, S., Wu, Y., Guillén-Samander, A., Hancock-Cerutti, W., Liu, J., & De Camilli, P. (2022). In situ architecture of the lipid transport protein VPS13C at ER-lysosome membrane contacts. Proceedings of the National Academy of Sciences, 119(29), e2203769119. https://doi.org/10.1073/pnas.2203769119
Caveney, N. A., Glassman, C. R., Jude, K. M., Tsutsumi, N., & Garcia, K. C. (2022). Structure of the IL-27 quaternary receptor signaling complex. eLife, 11. https://doi.org/10.7554/eLife.78463
den Boon, J. A., Zhan, H., Unchwaniwala, N., Horswill, M., Slavik, K., Pennington, J., Navine, A., & Ahlquist, P. (2022). Multifunctional Protein A Is the Only Viral Protein Required for Nodavirus RNA Replication Crown Formation. Viruses, 14(12), 2711. https://doi.org/10.3390/v14122711
Hirano, S., Kappel, K., Altae-Tran, H., Faure, G., Wilkinson, M. E., Kannan, S., Demircioglu, F. E., Yan, R., Shiozaki, M., Yu, Z., Makarova, K. S., Koonin, E. V., Macrae, R. K., & Zhang, F. (2022). Structure of the OMEGA nickase IsrB in complex with ωRNA and target DNA. Nature, 610(7932), 575–581. https://doi.org/10.1038/s41586-022-05324-6
Jeong, H., Clark, S., Goehring, A., Dehghani-Ghahnaviyeh, S., Rasouli, A., Tajkhorshid, E., & Gouaux, E. (2022). Structures of the TMC-1 complex illuminate mechanosensory transduction. Nature, 610(7933), 796–803. https://doi.org/10.1038/s41586-022-05314-8
Kumar, S., Zavaliev, R., Wu, Q., Zhou, Y., Cheng, J., Dillard, L., Powers, J., Withers, J., Zhao, J., Guan, Z., Borgnia, M. J., Bartesaghi, A., Dong, X., & Zhou, P. (2022). Structural basis of NPR1 in activating plant immunity. Nature, 605(7910), 561–566. https://doi.org/10.1038/s41586-022-04699-w
Shaban, N. M., Yan, R., Shi, K., Moraes, S. N., Cheng, A. Z., Carpenter, M. A., McLellan, J. S., Yu, Z., & Harris, R. S. (2022). Cryo-EM structure of the EBV ribonucleotide reductase BORF2 and mechanism of APOBEC3B inhibition. Science Advances, 8(17), eabm2827. https://doi.org/10.1126/sciadv.abm2827
Wang, L., Toutkoushian, H., Belyy, V., Kokontis, C. Y., & Walter, P. (2022). Conserved structural elements specialize ATAD1 as a membrane protein extraction machine. eLife, 11. https://doi.org/10.7554/eLife.73941
Warren, C., & Pavletich, N. P. (2022). Structure of the human ATM kinase and mechanism of Nbs1 binding. eLife, 11. https://doi.org/10.7554/eLife.74218
Wasmuth, E. V., Broeck, A. V., LaClair, J. R., Hoover, E. A., Lawrence, K. E., Paknejad, N., Pappas, K., Matthies, D., Wang, B., Feng, W., Watson, P. A., Zinder, J. C., Karthaus, W. R., de la Cruz, M. J., Hite, R. K., Manova-Todorova, K., Yu, Z., Weintraub, S. T., Klinge, S., & Sawyers, C. L. (2022). Allosteric interactions prime androgen receptor dimerization and activation. Molecular Cell, 82(11), 2021–2031.e5. https://doi.org/10.1016/j.molcel.2022.03.035
Wilson, S. C., Caveney, N. A., Yen, M., Pollmann, C., Xiang, X., Jude, K. M., Hafer, M., Tsutsumi, N., Piehler, J., & Garcia, K. C. (2022). Organizing structural principles of the IL-17 ligand-receptor axis. Nature, 609(7927), 622–629. https://doi.org/10.1038/s41586-022-05116-y
Zhou, K., Gebala, M., Woods, D., Sundararajan, K., Edwards, G., Krzizike, D., Wereszczynski, J., Straight, A. F., & Luger, K. (2022). CENP-N promotes the compaction of centromeric chromatin. Nature Structural & Molecular Biology, 29(4), 403–413. https://doi.org/10.1038/s41594-022-00758-y
Year 2021
Cao, Q., Boyer, D. R., Sawaya, M. R., Abskharon, R., Saelices, L., Nguyen, B. A., Lu, J., Murray, K. A., Kandeel, F., & Eisenberg, D. S. (2021). Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores. Nature Structural & Molecular Biology, 28(9), 724–730. https://doi.org/10.1038/s41594-021-00646-x
de Rus Jacquet, A., Tancredi, J. L., Lemire, A. L., DeSantis, M. C., Li, W.-P., & O’Shea, E. K. (2021). The LRRK2 G2019S mutation alters astrocyte-to-neuron communication via extracellular vesicles and induces neuron atrophy in a human iPSC-derived model of Parkinson’s disease. eLife, 10. https://doi.org/10.7554/eLife.73062
Elferich, J., Clark, S., Ge, J., Goehring, A., Matsui, A., & Gouaux, E. (2021). Molecular structures and conformations of protocadherin-15 and its complexes on stereocilia elucidated by cryo-electron tomography. eLife, 10. https://doi.org/10.7554/eLife.74512
Fukudome, A., Singh, J., Mishra, V., Reddem, E., Martinez-Marquez, F., Wenzel, S., Yan, R., Shiozaki, M., Yu, Z., Wang, J. C.-Y., Takagi, Y., & Pikaard, C. S. (2021). Structure and RNA template requirements of RNA-DEPENDENT RNA POLYMERASE 2. Proceedings of the National Academy of Sciences of the United States of America, 118(51). https://doi.org/10.1073/pnas.2115899118
Hao, Z., Epshtein, V., Kim, K. H., Proshkin, S., Svetlov, V., Kamarthapu, V., Bharati, B., Mironov, A., Walz, T., & Nudler, E. (2021). Pre-termination Transcription Complex: Structure and Function. Molecular Cell, 81(2), 281–292.e8. https://doi.org/10.1016/j.molcel.2020.11.013
Huang, Y., Ognjenovic, J., Karandur, D., Miller, K., Merk, A., Subramaniam, S., & Kuriyan, J. (2021). A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. eLife, 10. https://doi.org/10.7554/eLife.73218
Liou, S.-H., Singh, S. K., Singer, R. H., Coleman, R. A., & Liu, W.-L. (2021). Structure of the p53/RNA polymerase II assembly. Communications Biology, 4(1), 397. https://doi.org/10.1038/s42003-021-01934-4
Liu, Y., Bisio, H., Toner, C. M., Jeudy, S., Philippe, N., Zhou, K., Bowerman, S., White, A., Edwards, G., Abergel, C., & Luger, K. (2021). Virus-encoded histone doublets are essential and form nucleosome-like structures. Cell, 184(16), 4237–4250.e19. https://doi.org/10.1016/j.cell.2021.06.032
Markert, J., Zhou, K., & Luger, K. (2021). SMARCAD1 is an ATP-dependent histone octamer exchange factor with de novo nucleosome assembly activity. Science Advances, 7(42), eabk2380. https://doi.org/10.1126/sciadv.abk2380
Qiu, B., Matthies, D., Fortea, E., Yu, Z., & Boudker, O. (2021). Cryo-EM structures of excitatory amino acid transporter 3 visualize coupled substrate, sodium, and proton binding and transport. Science Advances, 7(10). https://doi.org/10.1126/sciadv.abf5814
Saxton, R. A., Tsutsumi, N., Su, L. L., Abhiraman, G. C., Mohan, K., Henneberg, L. T., Aduri, N. G., Gati, C., & Garcia, K. C. (2021). Structure-based decoupling of the pro- and anti-inflammatory functions of interleukin-10. Science (New York, N.Y.), 371(6535). https://doi.org/10.1126/science.abc8433
Sun, Y., Wang, J., Long, T., Qi, X., Donnelly, L., Elghobashi-Meinhardt, N., Esparza, L., Cohen, J. C., Xie, X.-S., Hobbs, H. H., & Li, X. (2021). Molecular basis of cholesterol efflux via ABCG subfamily transporters. Proceedings of the National Academy of Sciences of the United States of America, 118(34). https://doi.org/10.1073/pnas.2110483118
Xue, J., Han, Y., Baniasadi, H., Zeng, W., Pei, J., Grishin, N. V., Wang, J., Tu, B. P., & Jiang, Y. (2021). TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty acid elongase. eLife, 10. https://doi.org/10.7554/eLife.71220
Xue, J., Han, Y., Zeng, W., Wang, Y., & Jiang, Y. (2021). Structural mechanisms of gating and selectivity of human rod CNGA1 channel. Neuron, 109(8), 1302–1313.e4. https://doi.org/10.1016/j.neuron.2021.02.007
Yu, J., Zhu, H., Lape, R., Greiner, T., Du, J., Lü, W., Sivilotti, L., & Gouaux, E. (2021). Mechanism of gating and partial agonist action in the glycine receptor. Cell, 184(4), 957–968.e21. https://doi.org/10.1016/j.cell.2021.01.026
Year 2020
Anand, A. A., & Walter, P. (2020). Structural insights into ISRIB, a memory-enhancing inhibitor of the integrated stress response. The FEBS Journal, 287(2), 239–245. https://doi.org/10.1111/febs.15073
Gaullier, G., Roberts, G., Muthurajan, U. M., Bowerman, S., Rudolph, J., Mahadevan, J., Jha, A., Rae, P. S., & Luger, K. (2020). Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1. PloS One, 15(11), e0240932. https://doi.org/10.1371/journal.pone.0240932
He, S., Chou, H.-T., Matthies, D., Wunder, T., Meyer, M. T., Atkinson, N., Martinez-Sanchez, A., Jeffrey, P. D., Port, S. A., Patena, W., He, G., Chen, V. K., Hughson, F. M., McCormick, A. J., Mueller-Cajar, O., Engel, B. D., Yu, Z., & Jonikas, M. C. (2020). The structural basis of Rubisco phase separation in the pyrenoid. Nature Plants, 6(12), 1480–1490. https://doi.org/10.1038/s41477-020-00811-y
Isom, G. L., Coudray, N., MacRae, M. R., McManus, C. T., Ekiert, D. C., & Bhabha, G. (2020). LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope. Cell, 181(3), 653–664.e19. https://doi.org/10.1016/j.cell.2020.03.030
Lim, C. J., Barbour, A. T., Zaug, A. J., Goodrich, K. J., McKay, A. E., Wuttke, D. S., & Cech, T. R. (2020). The structure of human CST reveals a decameric assembly bound to telomeric DNA. Science (New York, N.Y.), 368(6495), 1081–1085. https://doi.org/10.1126/science.aaz9649
Park, J., Fu, Z., Frangaj, A., Liu, J., Mosyak, L., Shen, T., Slavkovich, V. N., Ray, K. M., Taura, J., Cao, B., Geng, Y., Zuo, H., Kou, Y., Grassucci, R., Chen, S., Liu, Z., Lin, X., Williams, J. P., Rice, W. J., Eng, E. T., Huang, R. K., Soni, R. K., Kloss, B., Yu, Z., Javitch, J. A., Hendrickson, W. A., Slesinger, P. A., Quick, M., Graziano, J., Yu, H., Fiehn, O., Clarke, O. B., Frank, J., & Fan, Q. R. (2020). Structure of human GABAB receptor in an inactive state. Nature, 584(7820), 304–309. https://doi.org/10.1038/s41586-020-2452-0
Rickgauer, J. P., Choi, H., Lippincott-Schwartz, J., & Denk, W. (2020). Label-free single-instance protein detection in vitrified cells. In bioRxiv. bioRxiv. https://doi.org/10.1101/2020.04.22.053868
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Year 2019
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Year 2018
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Gruszczyk, J., Huang, R. K., Chan, L.-J., Menant, S., Hong, C., Murphy, J. M., Mok, Y.-F., Griffin, M. D. W., Pearson, R. D., Wong, W., Cowman, A. F., Yu, Z., & Tham, W.-H. (2018). Cryo-EM structure of an essential Plasmodium vivax invasion complex. Nature, 559(7712), 135–139. https://doi.org/10.1038/s41586-018-0249-1
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Year 2017
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Hite, R. K., & MacKinnon, R. (2017). Structural Titration of Slo2.2, a Na+-Dependent K+ Channel. Cell, 168(3), 390–399.e11. https://doi.org/10.1016/j.cell.2016.12.030
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Liu, B., Hong, C., Huang, R. K., Yu, Z., & Steitz, T. A. (2017). Structural basis of bacterial transcription activation. Science (New York, N.Y.), 358(6365), 947–951. https://doi.org/10.1126/science.aao1923
Liu, D., Liu, X., Shang, Z., & Sindelar, C. V. (2017). Structural basis of cooperativity in kinesin revealed by 3D reconstruction of a two-head-bound state on microtubules. eLife, 6. https://doi.org/10.7554/eLife.24490
Liu, Y., Pan, J., Cai, Y., Grigorieff, N., Harrison, S. C., & Chen, B. (2017). Conformational States of a Soluble, Uncleaved HIV-1 Envelope Trimer. Journal of Virology, 91(10). https://doi.org/10.1128/JVI.00175-17
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Liu, Z., Gutierrez-Vargas, C., Wei, J., Grassucci, R. A., Sun, M., Espina, N., Madison-Antenucci, S., Tong, L., & Frank, J. (2017). Determination of the ribosome structure to a resolution of 2.5 Å by single-particle cryo-EM. Protein Science : A Publication of the Protein Society, 26(1), 82–92. https://doi.org/10.1002/pro.3068
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Tenthorey, J. L., Haloupek, N., López-Blanco, J. R., Grob, P., Adamson, E., Hartenian, E., Lind, N. A., Bourgeois, N. M., Chacón, P., Nogales, E., & Vance, R. E. (2017). The structural basis of flagellin detection by NAIP5: A strategy to limit pathogen immune evasion. Science (New York, N.Y.), 358(6365), 888–893. https://doi.org/10.1126/science.aao1140
Tocilj, A., On, K. F., Yuan, Z., Sun, J., Elkayam, E., Li, H., Stillman, B., & Joshua-Tor, L. (2017). Structure of the active form of human origin recognition complex and its ATPase motor module. eLife, 6. https://doi.org/10.7554/eLife.20818
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Year 2016
Abeyrathne, P. D., Koh, C. S., Grant, T., Grigorieff, N., & Korostelev, A. A. (2016). Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome. eLife, 5. https://doi.org/10.7554/eLife.14874
Briegel, A., Ortega, D. R., Mann, P., Kjær, A., Ringgaard, S., & Jensen, G. J. (2016). Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM. Proceedings of the National Academy of Sciences of the United States of America, 113(37), 10412–10417. https://doi.org/10.1073/pnas.1604693113
Chang, Y.-W., Rettberg, L. A., Treuner-Lange, A., Iwasa, J., Søgaard-Andersen, L., & Jensen, G. J. (2016). Architecture of the type IVa pilus machine. Science (New York, N.Y.), 351(6278), aad2001. https://doi.org/10.1126/science.aad2001
Cheng, T. C., Hong, C., Akey, I. V., Yuan, S., & Akey, C. W. (2016). A near atomic structure of the active human apoptosome. eLife, 5. https://doi.org/10.7554/eLife.17755
Hochstrasser, M. L., Taylor, D. W., Kornfeld, J. E., Nogales, E., & Doudna, J. A. (2016). DNA Targeting by a Minimal CRISPR RNA-Guided Cascade. Molecular Cell, 63(5), 840–851. https://doi.org/10.1016/j.molcel.2016.07.027
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Hussain, T., Llácer, J. L., Wimberly, B. T., Kieft, J. S., & Ramakrishnan, V. (2016). Large-Scale Movements of IF3 and tRNA during Bacterial Translation Initiation. Cell, 167(1), 133–144.e13. https://doi.org/10.1016/j.cell.2016.08.074
Jiang, F., Taylor, D. W., Chen, J. S., Kornfeld, J. E., Zhou, K., Thompson, A. J., Nogales, E., & Doudna, J. A. (2016). Structures of a CRISPR-Cas9 R-loop complex primed for DNA cleavage. Science (New York, N.Y.), 351(6275), 867–871. https://doi.org/10.1126/science.aad8282
Liu, Z., Gutierrez-Vargas, C., Wei, J., Grassucci, R. A., Ramesh, M., Espina, N., Sun, M., Tutuncuoglu, B., Madison-Antenucci, S., Woolford, J. L., Jr, Tong, L., & Frank, J. (2016). Structure and assembly model for the Trypanosoma cruzi 60S ribosomal subunit. Proceedings of the National Academy of Sciences of the United States of America, 113(43), 12174–12179. https://doi.org/10.1073/pnas.1614594113
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Mazhab-Jafari, M. T., Rohou, A., Schmidt, C., Bueler, S. A., Benlekbir, S., Robinson, C. V., & Rubinstein, J. L. (2016). Atomic model for the membrane-embedded Vo motor of a eukaryotic V-ATPase. Nature, 539(7627), 118–122. https://doi.org/10.1038/nature19828
Oldham, M. L., Grigorieff, N., & Chen, J. (2016). Structure of the transporter associated with antigen processing trapped by herpes simplex virus. eLife, 5. https://doi.org/10.7554/eLife.21829
Oldham, M. L., Hite, R. K., Steffen, A. M., Damko, E., Li, Z., Walz, T., & Chen, J. (2016). A mechanism of viral immune evasion revealed by cryo-EM analysis of the TAP transporter. Nature, 529(7587), 537–540. https://doi.org/10.1038/nature16506
Tajima, N., Karakas, E., Grant, T., Simorowski, N., Diaz-Avalos, R., Grigorieff, N., & Furukawa, H. (2016). Activation of NMDA receptors and the mechanism of inhibition by ifenprodil. Nature, 534(7605), 63–68. https://doi.org/10.1038/nature17679
Twomey, E. C., Yelshanskaya, M. V., Grassucci, R. A., Frank, J., & Sobolevsky, A. I. (2016). Elucidation of AMPA receptor-stargazin complexes by cryo-electron microscopy. Science (New York, N.Y.), 353(6294), 83–86. https://doi.org/10.1126/science.aaf8411
Wang, H., Cohen, A. A., Galimidi, R. P., Gristick, H. B., Jensen, G. J., & Bjorkman, P. J. (2016). Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop. Proceedings of the National Academy of Sciences of the United States of America, 113(46), E7151–E7158. https://doi.org/10.1073/pnas.1615939113
Worrall, L. J., Hong, C., Vuckovic, M., Deng, W., Bergeron, J. R. C., Majewski, D. D., Huang, R. K., Spreter, T., Finlay, B. B., Yu, Z., & Strynadka, N. C. J. (2016). Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body. Nature, 540(7634), 597–601. https://doi.org/10.1038/nature20576
Yuan, Z., Bai, L., Sun, J., Georgescu, R., Liu, J., O’Donnell, M. E., & Li, H. (2016). Structure of the eukaryotic replicative CMG helicase suggests a pumpjack motion for translocation. Nature Structural & Molecular Biology, 23(3), 217–224. https://doi.org/10.1038/nsmb.3170
Zhang, Z., & Chen, J. (2016). Atomic Structure of the Cystic Fibrosis Transmembrane Conductance Regulator. Cell, 167(6), 1586–1597.e9. https://doi.org/10.1016/j.cell.2016.11.014
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Year 2015
Du, J., Lü, W., Wu, S., Cheng, Y., & Gouaux, E. (2015). Glycine receptor mechanism elucidated by electron cryo-microscopy. Nature, 526(7572), 224–229. https://doi.org/10.1038/nature14853
Gonen, S., DiMaio, F., Gonen, T., & Baker, D. (2015). Design of ordered two-dimensional arrays mediated by noncovalent protein-protein interfaces. Science (New York, N.Y.), 348(6241), 1365–1368. https://doi.org/10.1126/science.aaa9897
Grant, T., & Grigorieff, N. (2015). Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6. eLife, 4, e06980. https://doi.org/10.7554/eLife.06980
Hite, R. K., Yuan, P., Li, Z., Hsuing, Y., Walz, T., & MacKinnon, R. (2015). Cryo-electron microscopy structure of the Slo2.2 Na+-activated K+ channel. Nature, 527(7577), 198–203. https://doi.org/10.1038/nature14958
Li, W., Liu, Z., Koripella, R. K., Langlois, R., Sanyal, S., & Frank, J. (2015). Activation of GTP hydrolysis in mRNA-tRNA translocation by elongation factor G. Science Advances, 1(4). https://doi.org/10.1126/sciadv.1500169
Taylor, D. W., Zhu, Y., Staals, R. H. J., Kornfeld, J. E., Shinkai, A., van der Oost, J., Nogales, E., & Doudna, J. A. (2015). Structural biology. Structures of the CRISPR-Cmr complex reveal mode of RNA target positioning. Science (New York, N.Y.), 348(6234), 581–585. https://doi.org/10.1126/science.aaa4535
Woodward, C. L., Cheng, S. N., & Jensen, G. J. (2015). Electron cryotomography studies of maturing HIV-1 particles reveal the assembly pathway of the viral core. Journal of Virology, 89(2), 1267–1277. https://doi.org/10.1128/JVI.02997-14
Year 2014
Briegel, A., Ladinsky, M. S., Oikonomou, C., Jones, C. W., Harris, M. J., Fowler, D. J., Chang, Y.-W., Thompson, L. K., Armitage, J. P., & Jensen, G. J. (2014). Structure of bacterial cytoplasmic chemoreceptor arrays and implications for chemotactic signaling. eLife, 3, e02151. https://doi.org/10.7554/eLife.02151
Briegel, A., Wong, M. L., Hodges, H. L., Oikonomou, C. M., Piasta, K. N., Harris, M. J., Fowler, D. J., Thompson, L. K., Falke, J. J., Kiessling, L. L., & Jensen, G. J. (2014). New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography. Biochemistry, 53(10), 1575–1585. https://doi.org/10.1021/bi5000614
Koh, C. S., Brilot, A. F., Grigorieff, N., & Korostelev, A. A. (2014). Taura syndrome virus IRES initiates translation by binding its tRNA-mRNA-like structural element in the ribosomal decoding center. Proceedings of the National Academy of Sciences of the United States of America, 111(25), 9139–9144. https://doi.org/10.1073/pnas.1406335111
Shikuma, N. J., Pilhofer, M., Weiss, G. L., Hadfield, M. G., Jensen, G. J., & Newman, D. K. (2014). Marine tubeworm metamorphosis induced by arrays of bacterial phage tail-like structures. Science (New York, N.Y.), 343(6170), 529–533. https://doi.org/10.1126/science.1246794
Svidritskiy, E., Brilot, A. F., Koh, C. S., Grigorieff, N., & Korostelev, A. A. (2014). Structures of yeast 80S ribosome-tRNA complexes in the rotated and nonrotated conformations. Structure (London, England : 1993), 22(8), 1210–1218. https://doi.org/10.1016/j.str.2014.06.003
Xu, H., He, X., Zheng, H., Huang, L. J., Hou, F., Yu, Z., de la Cruz, M. J., Borkowski, B., Zhang, X., Chen, Z. J., & Jiang, Q.-X. (2014). Structural basis for the prion-like MAVS filaments in antiviral innate immunity. eLife, 3, e01489. https://doi.org/10.7554/eLife.01489
Year 2013
Brilot, A. F., Korostelev, A. A., Ermolenko, D. N., & Grigorieff, N. (2013). Structure of the ribosome with elongation factor G trapped in the pretranslocation state. Proceedings of the National Academy of Sciences of the United States of America, 110(52), 20994–20999. https://doi.org/10.1073/pnas.1311423110