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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

Tsutsumi, N., Mukherjee, S., Waghray, D., Janda, C. Y., Jude, K. M., Miao, Y., Burg, J. S., Aduri, N. G., Kossiakoff, A. A., Gati, C., & Garcia, K. C. (2020). Structure of human Frizzled5 by fiducial-assisted cryo-EM supports a heterodimeric mechanism of canonical Wnt signaling. eLife, 9. https://doi.org/10.7554/eLife.58464

Unchwaniwala, N., Zhan, H., Pennington, J., Horswill, M., den Boon, J. A., & Ahlquist, P. (2020). Subdomain cryo-EM structure of nodaviral replication protein A crown complex provides mechanistic insights into RNA genome replication. Proceedings of the National Academy of Sciences of the United States of America, 117(31), 18680–18691. https://doi.org/10.1073/pnas.2006165117

Wu, X., Siggel, M., Ovchinnikov, S., Mi, W., Svetlov, V., Nudler, E., Liao, M., Hummer, G., & Rapoport, T. A. (2020). Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex. Science (New York, N.Y.), 368(6489). https://doi.org/10.1126/science.aaz2449

 

Year 2019

Dang, S., van Goor, M. K., Asarnow, D., Wang, Y., Julius, D., Cheng, Y., & van der Wijst, J. (2019). Structural insight into TRPV5 channel function and modulation. Proceedings of the National Academy of Sciences of the United States of America, 116(18), 8869–8878. https://doi.org/10.1073/pnas.1820323116

Feng, S., Dang, S., Han, T. W., Ye, W., Jin, P., Cheng, T., Li, J., Jan, Y. N., Jan, L. Y., & Cheng, Y. (2019). Cryo-EM Studies of TMEM16F Calcium-Activated Ion Channel Suggest Features Important for Lipid Scrambling. Cell Reports, 28(5), 1385. https://doi.org/10.1016/j.celrep.2019.07.052

Ghosal, D., Jeong, K. C., Chang, Y.-W., Gyore, J., Teng, L., Gardner, A., Vogel, J. P., & Jensen, G. J. (2019). Molecular architecture, polar targeting and biogenesis of the Legionella Dot/Icm T4SS. Nature Microbiology, 4(7), 1173–1182. https://doi.org/10.1038/s41564-019-0427-4

Ghosal, D., Kim, K. W., Zheng, H., Kaplan, M., Truchan, H. K., Lopez, A. E., McIntire, I. E., Vogel, J. P., Cianciotto, N. P., & Jensen, G. J. (2019). In vivo structure of the Legionella type II secretion system by electron cryotomography. Nature Microbiology, 4(12), 2101–2108. https://doi.org/10.1038/s41564-019-0603-6

Greber, B. J., Toso, D. B., Fang, J., & Nogales, E. (2019). The complete structure of the human TFIIH core complex. eLife, 8. https://doi.org/10.7554/eLife.44771

Griner, S. L., Seidler, P., Bowler, J., Murray, K. A., Yang, T. P., Sahay, S., Sawaya, M. R., Cascio, D., Rodriguez, J. A., Philipp, S., Sosna, J., Glabe, C. G., Gonen, T., & Eisenberg, D. S. (2019). Structure-based inhibitors of amyloid beta core suggest a common interface with tau. eLife, 8. https://doi.org/10.7554/eLife.46924

Heymann, J. B., Vijayasarathy, C., Huang, R. K., Dearborn, A. D., Sieving, P. A., & Steven, A. C. (2019). Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina. The Journal of Cell Biology, 218(3), 1027–1038. https://doi.org/10.1083/jcb.201806148

Hu, J., Worrall, L. J., Vuckovic, M., Hong, C., Deng, W., Atkinson, C. E., Brett Finlay, B., Yu, Z., & Strynadka, N. C. J. (2019). T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly. Nature Microbiology, 4(11), 2010–2019. https://doi.org/10.1038/s41564-019-0545-z

Kenner, L. R., Anand, A. A., Nguyen, H. C., Myasnikov, A. G., Klose, C. J., McGeever, L. A., Tsai, J. C., Miller-Vedam, L. E., Walter, P., & Frost, A. (2019). eIF2B-catalyzed nucleotide exchange and phosphoregulation by the integrated stress response. Science (New York, N.Y.), 364(6439), 491–495. https://doi.org/10.1126/science.aaw2922

Majewski, D. D., Worrall, L. J., Hong, C., Atkinson, C. E., Vuckovic, M., Watanabe, N., Yu, Z., & Strynadka, N. C. J. (2019). Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry. Nature Communications, 10(1), 626. https://doi.org/10.1038/s41467-019-08477-7

Nguyen, A. H., Thomsen, A. R. B., Cahill, T. J., 3rd, Huang, R., Huang, L.-Y., Marcink, T., Clarke, O. B., Heissel, S., Masoudi, A., Ben-Hail, D., Samaan, F., Dandey, V. P., Tan, Y. Z., Hong, C., Mahoney, J. P., Triest, S., Little, J., 4th, Chen, X., Sunahara, R., Steyaert, J., Molina, H., Yu, Z., des Georges, A., & Lefkowitz, R. J. (2019). Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex. Nature Structural & Molecular Biology, 26(12), 1123–1131. https://doi.org/10.1038/s41594-019-0330-y

Niekamp, S., Coudray, N., Zhang, N., Vale, R. D., & Bhabha, G. (2019). Coupling of ATPase activity, microtubule binding, and mechanics in the dynein motor domain. The EMBO Journal, 38(13), e101414. https://doi.org/10.15252/embj.2018101414

Shen, K., Rogala, K. B., Chou, H.-T., Huang, R. K., Yu, Z., & Sabatini, D. M. (2019). Cryo-EM Structure of the Human FLCN-FNIP2-Rag-Ragulator Complex. Cell, 179(6), 1319–1329.e8. https://doi.org/10.1016/j.cell.2019.10.036

Tao, X., & MacKinnon, R. (2019). Molecular structures of the human Slo1 K+ channel in complex with β4. eLife, 8. https://doi.org/10.7554/eLife.51409

Twomey, E. C., Ji, Z., Wales, T. E., Bodnar, N. O., Ficarro, S. B., Marto, J. A., Engen, J. R., & Rapoport, T. A. (2019). Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding. Science (New York, N.Y.), 365(6452). https://doi.org/10.1126/science.aax1033

Wong, W., Huang, R., Menant, S., Hong, C., Sandow, J. J., Birkinshaw, R. W., Healer, J., Hodder, A. N., Kanjee, U., Tonkin, C. J., Heckmann, D., Soroka, V., Søgaard, T. M. M., Jørgensen, T., Duraisingh, M. T., Czabotar, P. E., de Jongh, W. A., Tham, W.-H., Webb, A. I., Yu, Z., & Cowman, A. F. (2019). Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex. Nature, 565(7737), 118–121. https://doi.org/10.1038/s41586-018-0779-6

Wu, X., Cabanos, C., & Rapoport, T. A. (2019). Structure of the post-translational protein translocation machinery of the ER membrane. Nature, 566(7742), 136–139. https://doi.org/10.1038/s41586-018-0856-x

Zhang, Y., Cheng, T. C., Huang, G., Lu, Q., Surleac, M. D., Mandell, J. D., Pontarotti, P., Petrescu, A. J., Xu, A., Xiong, Y., & Schatz, D. G. (2019). Transposon molecular domestication and the evolution of the RAG recombinase. Nature, 569(7754), 79–84. https://doi.org/10.1038/s41586-019-1093-7

 

Year 2018

Bleichert, F., Leitner, A., Aebersold, R., Botchan, M. R., & Berger, J. M. (2018). Conformational control and DNA-binding mechanism of the metazoan origin recognition complex. Proceedings of the National Academy of Sciences of the United States of America, 115(26), E5906–E5915. https://doi.org/10.1073/pnas.1806315115

Close, W., Neumann, M., Schmidt, A., Hora, M., Annamalai, K., Schmidt, M., Reif, B., Schmidt, V., Grigorieff, N., & Fändrich, M. (2018). Physical basis of amyloid fibril polymorphism. Nature Communications, 9(1), 699. https://doi.org/10.1038/s41467-018-03164-5

Ge, J., Elferich, J., Goehring, A., Zhao, H., Schuck, P., & Gouaux, E. (2018). Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5. eLife, 7. https://doi.org/10.7554/eLife.38770

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

Hu, J., Worrall, L. J., Hong, C., Vuckovic, M., Atkinson, C. E., Caveney, N., Yu, Z., & Strynadka, N. C. J. (2018). Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin. Nature Communications, 9(1), 3840. https://doi.org/10.1038/s41467-018-06298-8

Hulse, R. E., Li, Z., Huang, R. K., Zhang, J., & Clapham, D. E. (2018). Cryo-EM structure of the polycystin 2-l1 ion channel. eLife, 7. https://doi.org/10.7554/eLife.36931

Jalali-Yazdi, F., Chowdhury, S., Yoshioka, C., & Gouaux, E. (2018). Mechanisms for Zinc and Proton Inhibition of the GluN1/GluN2A NMDA Receptor. Cell, 175(6), 1520–1532.e15. https://doi.org/10.1016/j.cell.2018.10.043

Jenni, S., & Harrison, S. C. (2018). Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface. Science (New York, N.Y.), 360(6388), 552–558. https://doi.org/10.1126/science.aar6436

Kasinath, V., Faini, M., Poepsel, S., Reif, D., Feng, X. A., Stjepanovic, G., Aebersold, R., & Nogales, E. (2018). Structures of human PRC2 with its cofactors AEBP2 and JARID2. Science (New York, N.Y.), 359(6378), 940–944. https://doi.org/10.1126/science.aar5700

Kim, S. J., Fernandez-Martinez, J., Nudelman, I., Shi, Y., Zhang, W., Raveh, B., Herricks, T., Slaughter, B. D., Hogan, J. A., Upla, P., Chemmama, I. E., Pellarin, R., Echeverria, I., Shivaraju, M., Chaudhury, A. S., Wang, J., Williams, R., Unruh, J. R., Greenberg, C. H., Jacobs, E. Y., Yu, Z., de la Cruz, M. J., Mironska, R., Stokes, D. L., Aitchison, J. D., Jarrold, M. F., Gerton, J. L., Ludtke, S. J., Akey, C. W., Chait, B. T., Sali, A., & Rout, M. P. (2018). Integrative structure and functional anatomy of a nuclear pore complex. Nature, 555(7697), 475–482. https://doi.org/10.1038/nature26003

Kim, Y., & Chen, J. (2018). Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation. Science (New York, N.Y.), 359(6378), 915–919. https://doi.org/10.1126/science.aar7389

Kintzer, A. F., Green, E. M., Dominik, P. K., Bridges, M., Armache, J.-P., Deneka, D., Kim, S. S., Hubbell, W., Kossiakoff, A. A., Cheng, Y., & Stroud, R. M. (2018). Structural basis for activation of voltage sensor domains in an ion channel TPC1. Proceedings of the National Academy of Sciences of the United States of America, 115(39), E9095–E9104. https://doi.org/10.1073/pnas.1805651115

Regan, M. C., Grant, T., McDaniel, M. J., Karakas, E., Zhang, J., Traynelis, S. F., Grigorieff, N., & Furukawa, H. (2018). Structural Mechanism of Functional Modulation by Gene Splicing in NMDA Receptors. Neuron, 98(3), 521–529.e3. https://doi.org/10.1016/j.neuron.2018.03.034

Ruhe, Z. C., Subramanian, P., Song, K., Nguyen, J. Y., Stevens, T. A., Low, D. A., Jensen, G. J., & Hayes, C. S. (2018). Programmed Secretion Arrest and Receptor-Triggered Toxin Export during Antibacterial Contact-Dependent Growth Inhibition. Cell, 175(4), 921–933.e14. https://doi.org/10.1016/j.cell.2018.10.033

Shen, K., Huang, R. K., Brignole, E. J., Condon, K. J., Valenstein, M. L., Chantranupong, L., Bomaliyamu, A., Choe, A., Hong, C., Yu, Z., & Sabatini, D. M. (2018). Architecture of the human GATOR1 and GATOR1-Rag GTPases complexes. Nature, 556(7699), 64–69. https://doi.org/10.1038/nature26158

Sui, X., Arlt, H., Brock, K. P., Lai, Z. W., DiMaio, F., Marks, D. S., Liao, M., Farese, R. V., Jr, & Walther, T. C. (2018). Cryo-electron microscopy structure of the lipid droplet-formation protein seipin. The Journal of Cell Biology, 217(12), 4080–4091. https://doi.org/10.1083/jcb.201809067

Tsai, J. C., Miller-Vedam, L. E., Anand, A. A., Jaishankar, P., Nguyen, H. C., Renslo, A. R., Frost, A., & Walter, P. (2018). Structure of the nucleotide exchange factor eIF2B reveals mechanism of memory-enhancing molecule. Science (New York, N.Y.), 359(6383). https://doi.org/10.1126/science.aaq0939

Wang, H., Barnes, C. O., Yang, Z., Nussenzweig, M. C., & Bjorkman, P. J. (2018). Partially open HIV-1 envelope structures exhibit conformational changes relevant for coreceptor binding and fusion. Cell Host & Microbe, 24(4), 579–592.e4. https://doi.org/10.1016/j.chom.2018.09.003

White, K. I., Zhao, M., Choi, U. B., Pfuetzner, R. A., & Brunger, A. T. (2018). Structural principles of SNARE complex recognition by the AAA+ protein NSF. eLife, 7. https://doi.org/10.7554/eLife.38888

Zhang, Y., Bulkley, D. P., Xin, Y., Roberts, K. J., Asarnow, D. E., Sharma, A., Myers, B. R., Cho, W., Cheng, Y., & Beachy, P. A. (2018). Structural Basis for Cholesterol Transport-like Activity of the Hedgehog Receptor Patched. Cell, 175(5), 1352–1364.e14. https://doi.org/10.1016/j.cell.2018.10.026

 

Year 2017

Alewijnse, B., Ashton, A. W., Chambers, M. G., Chen, S., Cheng, A., Ebrahim, M., Eng, E. T., Hagen, W. J. H., Koster, A. J., López, C. S., Lukoyanova, N., Ortega, J., Renault, L., Reyntjens, S., Rice, W. J., Scapin, G., Schrijver, R., Siebert, A., Stagg, S. M., Grum-Tokars, V., Wright, E. R., Wu, S., Yu, Z., Zhou, Z. H., Carragher, B., & Potter, C. S. (2017). Best practices for managing large CryoEM facilities. Journal of Structural Biology, 199(3), 225–236. https://doi.org/10.1016/j.jsb.2017.07.011

Cheng, T. C., Akey, I. V., Yuan, S., Yu, Z., Ludtke, S. J., & Akey, C. W. (2017). A Near-Atomic Structure of the Dark Apoptosome Provides Insight into Assembly and Activation. Structure (London, England : 1993), 25(1), 40–52. https://doi.org/10.1016/j.str.2016.11.002

Dang, S., Feng, S., Tien, J., Peters, C. J., Bulkley, D., Lolicato, M., Zhao, J., Zuberbühler, K., Ye, W., Qi, L., Chen, T., Craik, C. S., Jan, Y. N., Minor, D. L., Jr, Cheng, Y., & Jan, L. Y. (2017). Cryo-EM structures of the TMEM16A calcium-activated chloride channel. Nature, 552(7685), 426–429. https://doi.org/10.1038/nature25024

Demo, G., Rasouly, A., Vasilyev, N., Svetlov, V., Loveland, A. B., Diaz-Avalos, R., Grigorieff, N., Nudler, E., & Korostelev, A. A. (2017). Structure of RNA polymerase bound to ribosomal 30S subunit. eLife, 6. https://doi.org/10.7554/eLife.28560

Ekiert, D. C., Bhabha, G., Isom, G. L., Greenan, G., Ovchinnikov, S., Henderson, I. R., Cox, J. S., & Vale, R. D. (2017). Architectures of Lipid Transport Systems for the Bacterial Outer Membrane. Cell, 169(2), 273–285.e17. https://doi.org/10.1016/j.cell.2017.03.019

Ertel, K. J., Benefield, D., Castaño-Diez, D., Pennington, J. G., Horswill, M., den Boon, J. A., Otegui, M. S., & Ahlquist, P. (2017). Cryo-electron tomography reveals novel features of a viral RNA replication compartment. eLife, 6. https://doi.org/10.7554/eLife.25940

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

Hite, R. K., Tao, X., & MacKinnon, R. (2017). Structural basis for gating the high-conductance Ca2+-activated K+ channel. Nature, 541(7635), 52–57. https://doi.org/10.1038/nature20775

Jin, P., Bulkley, D., Guo, Y., Zhang, W., Guo, Z., Huynh, W., Wu, S., Meltzer, S., Cheng, T., Jan, L. Y., Jan, Y.-N., & Cheng, Y. (2017). Electron cryo-microscopy structure of the mechanotransduction channel NOMPC. Nature, 547(7661), 118–122. https://doi.org/10.1038/nature22981

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

Liu, Y., Pan, J., Jenni, S., Raymond, D. D., Caradonna, T., Do, K. T., Schmidt, A. G., Harrison, S. C., & Grigorieff, N. (2017). CryoEM Structure of an Influenza Virus Receptor-Binding Site Antibody-Antigen Interface. Journal of Molecular Biology, 429(12), 1829–1839. https://doi.org/10.1016/j.jmb.2017.05.011

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

Loveland, A. B., Demo, G., Grigorieff, N., & Korostelev, A. A. (2017). Ensemble cryo-EM elucidates the mechanism of translation fidelity. Nature, 546(7656), 113–117. https://doi.org/10.1038/nature22397

Pentakota, S., Zhou, K., Smith, C., Maffini, S., Petrovic, A., Morgan, G. P., Weir, J. R., Vetter, I. R., Musacchio, A., & Luger, K. (2017). Decoding the centromeric nucleosome through CENP-N. eLife, 6. https://doi.org/10.7554/eLife.33442

Rickgauer, J. P., Grigorieff, N., & Denk, W. (2017). Single-protein detection in crowded molecular environments in cryo-EM images. eLife, 6. https://doi.org/10.7554/eLife.25648

Schoebel, S., Mi, W., Stein, A., Ovchinnikov, S., Pavlovicz, R., DiMaio, F., Baker, D., Chambers, M. G., Su, H., Li, D., Rapoport, T. A., & Liao, M. (2017). Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3. Nature, 548(7667), 352–355. https://doi.org/10.1038/nature23314

Shin, J., Jiang, F., Liu, J.-J., Bray, N. L., Rauch, B. J., Baik, S. H., Nogales, E., Bondy-Denomy, J., Corn, J. E., & Doudna, J. A. (2017). Disabling Cas9 by an anti-CRISPR DNA mimic. Science Advances, 3(7), e1701620. https://doi.org/10.1126/sciadv.1701620

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

Twomey, E. C., Yelshanskaya, M. V., Grassucci, R. A., Frank, J., & Sobolevsky, A. I. (2017). Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes. Neuron, 94(3), 569–580.e5. https://doi.org/10.1016/j.neuron.2017.04.025

Wang, H., Gristick, H. B., Scharf, L., West, A. P., Galimidi, R. P., Seaman, M. S., Freund, N. T., Nussenzweig, M. C., & Bjorkman, P. J. (2017). Asymmetric recognition of HIV-1 Envelope trimer by V1V2 loop-targeting antibodies. eLife, 6. https://doi.org/10.7554/eLife.27389

Yuan, Z., Riera, A., Bai, L., Sun, J., Nandi, S., Spanos, C., Chen, Z. A., Barbon, M., Rappsilber, J., Stillman, B., Speck, C., & Li, H. (2017). Structural basis of Mcm2-7 replicative helicase loading by ORC-Cdc6 and Cdt1. Nature Structural & Molecular Biology, 24(3), 316–324. https://doi.org/10.1038/nsmb.3372

Zeytuni, N., Hong, C., Flanagan, K. A., Worrall, L. J., Theiltges, K. A., Vuckovic, M., Huang, R. K., Massoni, S. C., Camp, A. H., Yu, Z., & Strynadka, N. C. (2017). Near-atomic resolution cryoelectron microscopy structure of the 30-fold homooligomeric SpoIIIAG channel essential to spore formation in Bacillus subtilis. Proceedings of the National Academy of Sciences of the United States of America, 114(34), E7073–E7081. https://doi.org/10.1073/pnas.1704310114

Zhou, C. Y., Stoddard, C. I., Johnston, J. B., Trnka, M. J., Echeverria, I., Palovcak, E., Sali, A., Burlingame, A. L., Cheng, Y., & Narlikar, G. J. (2017). Regulation of Rvb1/Rvb2 by a Domain within the INO80 Chromatin Remodeling Complex Implicates the Yeast Rvbs as Protein Assembly Chaperones. Cell Reports, 19(10), 2033–2044. https://doi.org/10.1016/j.celrep.2017.05.029

 

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

Hsia, Y., Bale, J. B., Gonen, S., Shi, D., Sheffler, W., Fong, K. K., Nattermann, U., Xu, C., Huang, P.-S., Ravichandran, R., Yi, S., Davis, T. N., Gonen, T., King, N. P., & Baker, D. (2016). Design of a hyperstable 60-subunit protein dodecahedron. Nature, 535(7610), 136–139. https://doi.org/10.1038/nature18010

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

Loveland, A. B., Bah, E., Madireddy, R., Zhang, Y., Brilot, A. F., Grigorieff, N., & Korostelev, A. A. (2016). Ribosome•RelA structures reveal the mechanism of stringent response activation. eLife, 5. https://doi.org/10.7554/eLife.17029

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