Skip to main content
SLAC National Accelerator Laboratory
S2C2Stanford-SLAC CryoEM Center

Main navigation

  • About
    • People
      • S2C2 Staff
      • S2C2 Advisory Board
      • S2C2 Project Review Committee
    • Contacts for Cryo-EM Services
    • S2C2 Organization Chart
  • Facilities
  • User Access
    • User Information
      • Project Evaluation Criteria
      • Project Application Materials
      • Time Request Materials
      • Data Access and Transfer
    • Process for Accessing S2C2 CryoEM Resources
  • Training
    • CryoEM Training Curriculum
    • Project-tailored CryoEM Training Program
    • Comprehensive CryoEM Training Program
    • Workshops & Lectures
      • Workshop & Lecture Archive
    • CryoEM Training Videos
  • Publications
    • Acknowledgement Requirement
    • Publications 2025
    • Publications 2024
    • Publications 2023
    • Publications 2022
    • Publications 2021
    • Publications 2020
    • Publications 2019
  • FAQs

Breadcrumb

  1. Home
  2. …
Facebook Share X Post LinkedIn Share Email Send
  • Acknowledgement Requirement
  • Publications 2025
  • Publications 2024
  • Publications 2023
  • Publications 2022
  • Publications 2021
  • Publications 2020
  • Publications 2019

Publications by Year

These publications have resulted from work performed at the Stanford-SLAC CryoEM Center (S2C2), which is supported by the National Institutes of Health Common Fund Transformative High-Resolution Cryo-Electron Microscopy Program. 

Zhang, M.; Nam, Y.-W; Ramanishka, A.; Xu, Y.; Yasuda, R.M.; Im, D.; Cui, M.; Chandy, G.; Wulff, H.; 
     Structural basis for the subtype-selectivity of KCa2.2 channel activators Nature Portfolio; 
     (Preprint), https://doi.org/10.21203/rs.3.rs-6568445/v1
Mietzsch, M.; Hsi, J.; Nelson, A.R.; Khandekar, N.; Huang, A.-M.; Smith, N.J.C.; Zachary, J.; Potts, L.; 
     Farrar, M.A.; Chipman, P.; Ghanem, M.; Alexander, I.E.; Logan, G.J.; Huiskonen, J.T.; McKenna, R.;
     Structural characterization of antibody-responses following Zolgensma treatment for AAV
     capsid engineering to expand patient cohorts. Nature Communications; 19 April 2025 16, 1, 3731
     https://doi.org/10.1038/s41467-025-59088-4
Nam, Y.-W.; Im, D.; Garcia, A.S.C.; Tringides, M.L.; Nguyen, H.M.; Liu, Y.; Orfali, R.; Ramanishka, A.;
    Pintilie, G.; Su, C.-C.; Cui, M.; Logothetis, D.E.; Yu, E.W.; Wulff, H.; Chandy, K.G.; Zhang, M.; 
    Cryo-EM structures of the small-conductance Ca2+-activated KCa2.2 channel. Nature
    Communications; 17 April 2025 16, 3690 https://doi.org/10.1038/s41467-025-59061-1
Varanese, L.; Xu, L.; Peters. C.E.; Pintilie, G.; Roberts, D.S.; Raj, S.; Liu, M.; Ooi, Y.S.; Diep, J.; Qiao, W.; 
    Richards, C.M.; Callaway, J.; Bertozzi, C.R.; Jabs, S.; de Vries, E.; van Kuppeveld, F.J.M.;  Nagamine, C.M;
    Chiu, W.; Carette, J.E.; MFSD6 is an entry receptor for enterovirus D68. Nature; 25 March 2025 
     https://doi.org/10.1038/s41586-025-08908-0
Nayak, A.R.; Sokolova, V.; Sillamaa, S.; Herbine, K.; Sedman, J.; Temiakov, D.; Structural basis for
    intrinsic strand displacement activity of mitochondrial DNA polymerase. Nature Communications
    11 March 2025 16(2417) https://doi.org/10.1038/s41467-025-57594-z
He, Z.; Zhang, J.; Xu, Y.; Fine, E.J.; Suomivuori, C.-M.; Dror, R.O.; Feng, L.;  Structure of mitochondrial 
     pyruvate carrier and its inhibition mechanism. Nature; 5 March 2025 
     https://doi.org/10.1038/s41586-025-08667-y 
Rubio, A.A.; Baharani, V.A.; Dadonaite, B.; Parada, M.; Abernathy, M.E.; Wang, Z.; Lee, Y.E.; Eso, M.R.; 
     Jennie, P.; Ramos, I.; Chen, T.; El Nesr, G.; Bloom, J.D.; Bieniasz, P.D.; Nussenzweig, M.C.; Barnes, C.O.;
     Bispecific antibodies targeting the N-terminal and receptor binding domains potently
     neutralize SARS-CoV-2 variants of concern. Science Translational Medicine; 5 March 2025 17(788)
     doi: 10.1126/scitranslmed.adq5720
Wang, K.; Li, L.; Kenny, S.; Gan, D.; Reistma, J.M.; Zhou, Y.; Das, C.; Liu, X.; Molecular mechanisms
    of CAND2 in regulating SCF ubiquitin ligases. Nature Communications; 26 February 25 1998(16)1
    DOI: https://doi.org/10.1038/s41467-025-57065-5
Zhang, Z.; Chiang, H.T.; Xia, Y.; Avakyan, N.; Sonani, R.R.; Wang, F.; Egelman, E.H.; De Yoreo, J.J.; Pozzo,
     L.D.; Tezcan, F.A.; Design of light- and chemically responsive protein assemblies through host-
     guest interactions. Chem; 10 February 2025 https://doi.org/10.1016/j.chempr.2024.102407
Gliwa, K.; Hull, J.; Kansol, A.; Zembruski, V.; Lakshmanan, R.; Mietzsch, M.; Chipman, P.; Bennett, A.; 
    McKenna, R.; Biophysical and structural insights into AAV genome ejection. Journal of Virology; 
    5 February 2025 Biophysical and structural insights into AAV genome ejection
Zhao, Y.; Vidossich, P.; Forbush, B.; Ma, J.; Rinehart, J.; De Vivo, M.; Cao, E.; Structural basis for 
     human NKCC1 inhibition by loop diuretic drugs. EMBO Journal; 28 January 2025 
     DOI: 10.1038/s44318-025-00368-6
Kretsch, R.C.; Li, S.; Pintilie, G.; Palo, M.Z.; Case, D.A.; Das, R.; Zhang,K.; Chiu,W.; Complex Water 
    Networks Visualized through 2.2-2.3 Å Cryogenic Electron Microscopy of RNA. bioRxiv (Preprint)
    24 January 2025 doi: https://doi.org/10.1101/2025.01.23.634578
Li, Y.; Zhu, J.; Zhang, Z.; Wei, J.; Wang, F.; Meisl, G.; Knowles, T.P.J.; Egelman, E.H.; Tezcan, A.;  
    Transforming an ATP-dependent enzyme into a dissipative, self-assembling system. Nature 
    Chemical Biology 13 January 2025 1552-4469; https://doi.org/10.1038/s41589-024-01811-1
Ganguly, C.; Martin, L.; Aribam, S.; Thomas, L.M.; Rajan, R.; Helical transition of the bridge helix 
    of Cas12a is an allosteric regulator of R-loop formation and RuvC activation. bioRxiv (Preprint) 
    10 January 2025 https://www.biorxiv.org/content/10.1101/2025.01.09.632262v1
Jabbari, K.; Mietzach, M.; Hsi, J.; Chipman, P.; Qiu, J.; McKenna, R.; The Structural, Biophysical, and 
    Antigenic Characterization of the Goose Parvovirus Capsid. Microorganisms 3 January 2025 13(1),80; 
    https://doi.org/10.3390/microorganisms13010080
Deng, X.; Sun, L.; Zhang, M.; Basavaraj, R.; Wang, J.; Weng, Y.-L.; Gao, Y.; Biochemical Profiling and 
    Structural Basis of ADAR1-Mediated RNA Editing. bioRxiv (Preprint) 2 January 2025

de March, C.A.; Ma, N.; Billesbolle, C.B.; Tewari, J.; del Torrent, C.L.; van der Velden, W.J.C.; Ojiro, I.; 
     Takayama, I.; Faust, B.; Li, L.; Vaidehi, N.; Manglik, A.; Matsunami, H.; Engineered odorant 
     receptors illuminate the basis of odour discrimination. Nature 30 October 2024 
     DOI: https://doi.org/10.1038/s41586-024-08126-0
Nguyen, B.A.; Afrin, S.; Yakubovska, A.; Singh, V.; Pedretti, R.; Bassett, P.; Pekala, M; Alicea, J.V.; 
      Kunach, P.; Wang, Lanie; Lemoff, A.; Kluve-Beckerman, B.; Saelices, L.; ATTRv-V30M amyloid 
      fibrils from heart and nerves exhibit structural homogeneity. Structure 17 October 2024 
      https://doi.org/10.1016/j.str.2024.09.021
Cogan, D.P.; Soohoo, A.M.; Chen, M.; Liu, Y.; Brodsky, K.L.; Khosla, Chaitan; Structural basis for
      intermodular communication in assembly-line polyketide biosynthesis. Nature Chemical  
      Biology 23 August 2023 DOI: https://doi.org/10.1038/s41589-024-01709-y
Zhao, Y.; Schubert, H.; Blakely, A.; Forbush, B.; Smith, M.D.; Rinehart, J.; Cao, E.; Structural bases 
      for Na+-Cl− cotransporter  inhibition by thiazide diuretic drugs and activation by kinases. Nature 
      Communications 14 August 2024 15(1)7006 DOI: https://doi.org/10.1038/s41467-024-51381-y
Held, R.G.; Liang, J.; Brunger, A.T.; Nanoscale architecture of synaptic vesicles and scaffolding 
     complexes revealed by cryo-electron tomography. Neuroscience 26 June 2024 121(27) DOI: 
     https://doi.org/10.1073/pnas.2403136121
Chien, C.-T.; Puhl, H.; Vogel, S.S.; Molloy, J.E.; Chiu, W.; Khan, S.; Hub stability in the calcium 
     calmodulin-dependent protein kinase II. Communications Biology 25 June 2024 7(766) 
     DOI: https://doi.org/10.1038/s42003-024-06423-y
Suryadevara, N.; Otrelo-Cardoso, A.R.; Kose, N.; Hu, Y.-X.; Binshtein, E.; Wolters, R.M.; Greninger, A.L.;
     Handal, L.S.; Carnahan, R.H.; Moscona, A.; Jardetsky, T.S.; Crowe, Jr., J.E.: Functional and structural 
     basis of human parainfluenza virus type 3 neutralization with human monoclonal antibodies. 
     Nature Microbiology 10 June 2024 DOI: https://doi.org/10.1038/s41564-024-01722-w
Park, J.; Herrmann, G.K.; Roy, A.; Shumate, C.K.; Cisneros, G.A.; Yin, Y.W.; An interaction network 
     in the polymerase active site is a prerequisite for Watson-Crick base pairing in Pol γ. Science 
    Advances 24 May 2024, 10(21) DOI: 10.1126/sciadv.adl3214
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.; How short peptides can disassemble
    ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism. 
    Nature Portfolio (Preprint 05.08.24 ) DOI: https://doi.org/10.21203/rs.3.rs-4152095/v1
 Chew, B.L.A.; Ngoh, A.Q.; Phoo, W.W.; Weng, M.J.G.; Shen, H.J.; Chan, K.W.K.; Tan, E.Y.J.; Gelbart, T.;
      Xu, C.; Tan, G.S.; Vasudevan, S.G.; Luo, D.; Structural basis of Zika virus NS1 multimerization and 
      human antibody recognition. NPJ Viruses 25 April 2024, 2(1) 
      https://doi.org/10.1038/s44298-024-00024-6 page 14
Thongchol, J.; Yu, Z.; Harb, L.; Lin, Y.; Koch, M.; Theodore, M.; Narsaria, U.; Shaevitz, J.; Gitai, Z.; 
     Wu, Y.; Zhang, J.; Zeng, L.; Removal of Pseudomonas type IV pili by a small RNA virus. Science 5 
      April 2024, 384(6691) https://doi.org/10.1126/science.adl0635
Balana, A.T.; Mahul-Mellier, A.-L.; Nguyen, B.A.; Horvath, M.; Javed, A.; Hard, E.R.; Jasiqi, Y.; Singh, P.; 
      Afrin, S.; Pedretti, R.; Singh, V.; Lee, V.M.-Y.; Luk, K.C.; Saelices, L.; Lashuel H.A.; Pratt, M.R.; 
      O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology. 
      Nature Chemical Biology 12 February 2024, https://doi.org/10.1038/s41589-024-01551-2
Cookis, T.; Lydecker, A.; Sauer, P.; Kasinath, V.; Nogales, E.; Structural basis for the inhibition of PRC2
      by active transcription histone posttranslational modifications. bioRxiv preprint 10 February 2024, 
      https://doi.org/10.1101/2024.02.09.579730
Sharma, S.; Luo, M.; Patel, H.; Mueller, D.M.; Liao, M.; Conformational ensemble of yeast ATP synthase
      at low pH reveals unique intermediates and plasticity in F1–Fo coupling. Nature Structural & 
      Molecular Biology 5 February 2024, 1545-9985 https://doi.org/10.1038/s41594-024-01219-4
Masse, M.M.; Hutchinson, R.B.; Morgan, C.E.; Allaman, H.J.; Guan, H.; Yu, E.W.; Cavagnero, S.; Mapping
      Protein–Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome–Nascent
      Globin Complex. ASC Cent. Sci. XXXX, XXX, XXX-XXX 1 February 2024; 
      https://doi.org/10.1021/acscentsci.3c00777
Nguyen, B.A.; Singh, V.; Afrin, S.; Yakubovska, A.; Wang, L.; Ahmed, Y.; Pedretti, R.; Fernandez-Ramirez,
      M.D.C.; Sing, P.; Pekala, M. Cabrera Hernandez, L.O.; Kumar, S.; Lemoff, A.; Gonzalez-Prieto, R.;
      Sawaya, M.R.; Eisenberg, D.S.; Benson, M.D.; Saelices, L.; Structural polymorphism of amyloid 
      fibrils in ATTR amyloidosis revealed by cryo-electron microscopy. Nature Communications |
      17 January 2024; 15, 581; https://doi.org/10.1038/s41467-024-44820-3
Yang, R.; Ko, Y.-H.; Li, F.; Lokareddy, R.K.; Hou, C.-F. D.; Kim, C.; Klein, S.; Antolinez, S.; Marin, J.F.; 
      Perez-Segura, C.; Jarrold, M.F.; Zlotnick, A.; Hadden-Perilla, J.A.; Cingolani, G.; Structural basis 
      for nuclear import of hepatitis B virus (HBV) nucleocapsid core. Science Advances 10 January 2024; 
      10:2; DOI:10.1126/sciadv.adi7606
Wang, L.; Hoang, A.; Gil-lturbe, E.; Laganowsky, A.; Quick, M.; Zhou, M.; Mechanism of anion exchange
      and small-molecule inhibition of pendrin. Nature Communications 01 January 2024; 15:346;
      https://doi.org/10.1038/s41467-023-44612-1

 

Shen, Z.; Lin, Q.; Yang, X-Y.; Fosuah, E.; Fu, T-M.; Assembly-mediated activation of the SIR2-HerA supramolecular complex
        for anti-phage defense. Molecular Cell 21 December 2023; 83, 24; https://doi.org/10.1016/j.molcel.2023.11.007
Oh, J.; Shan, Z.; Hoshika, S.; Xu, J.; Chong, J.; Benner, S.A.; Lyumkis, D.; Wang, D.; A unified Watson-Crick geometry drives 
        transcription of six-letter expanded DNA alphabets by E. coli RNA polymerase. Nature Communications 12 December 2023;
        14,8219; https://doi.org/10.1038/s41467-023-43735-9
Rosenberg, G.M.; Abskharon, R.; Boyer, D.R.; Ge, P.; Sawaya, M.R.; Eisenberg, D.S.; Fibril structures of TFG Protein
        mutants validate identification of TFG as a disease-related amyloid protein by the IMPAcT method. PNAS Nexus 
        20 November 2023; pgad402; https://doi.org/10.1093/pnasnexus/pgad402
Liu, Q.; Stadtmueller, B.M.; SIgA structures bound to Streptococcus pyogenes M4 and human CD89 provide insights 
         into host-pathogen interactions. Nature Communications 23 October 2023; https://doi.org/10.1038/s41467-023-42469-y
Gangwar, S.P.;Yen, L.Y.; Yelshanskaya, M.V., Korman, A.; Jones, D.R.; Sobolevsky A.I.; Modulation of GluA2-γ5 synaptic complex 
         desensitization, polyamine block and antiepileptic perampanel inhibition by auxiliary subunit cornichon-2. Natural 
         Structural & Molecular Biology 31, August 2023, https://doi.org/10.1038/s41594-023-01080-x
Velez, M.; Mietzsch, M.; Hsi, J.; Bell, L.; Chipman, P.; Fu, X.; McKenna, R.; Structural Characterization of Canine Minute Virus, 
        Rat, and Porcine Bocavirus. Viruses, 24 August 2023, 15(9), 1799; https://doi.org/10.3390/v15091799 
Logan, G.J.; Mietzsch, M.; Khandekar, N.; D'Silva, A.; Anderson, D.; Mandwie, M.; Hsi, J.; Nelson, A.R.; Chipman, P.; Jackson, J.; 
         Schofield, P.; Christ, D.; Goodnow, C.C.; Reed, J.H.; Farrar, M.A.; McKenna, R.; Alexander, I.E.; Structural and functional 
         characterization of capsid binding by anti-AAV9 monoclonal antibodies from infants after SMA gene therapy. Molecular 
         Therapy, 2023, doi: https://doi.org/10.1016/j.ymthe.2023.03.032
Zimanyi, C.M.; Rayaprolu, V.; Keeping up with Current Practices in a Rapidly Evolving Field Through Dissemination of 
         "Tips and Tricks" in a Monthly Webinar. Microscopy Today, 31 May 2023, Volume 31, Issue 3, Pages 28-33, 
         https://doi.org/10.1093/mictod/qaad024 
Park, J.; Herrmann, G.K.; Mitchell, P.G.; Sherman, M.B.; Yin, Y.W.; Poly coordinates DNA synthesis and proofreading to 
         ensure mitochondrial genome integrity. Nature Structural & Molecular Biology, 18 May 2023, doi: 
         https://doi.org/10.1038/s41594-023-00980-2
Chen, Z.; Monda, A.; Ali, F.A.; Jang, S.; Niranjan, S.; Montaño, J.L.; Zaro, B.W.; Minor, D.L.; EMC chaperone-Cav structure 
         reveals an ion channel assembly intermediate. Nature 17 May 2023, doi: https//doi.org/10.1038/s41586-023-06175-5
Gupta, A.M.; Lentzsch, A.M.; Siegel, A.; Yu, Z.; Chio, U.S.; Cheng, Y.; Shan, S.-O.; Dodecamer assembly of a metazoan AAA+
         chaperone couples substrate extraction to refolding. Science Advances, 10 May 2023, 9(19), DOI: 10.1126/sciadv.adf5336
Weidenbacher, P. A.-B.; Sanyal, M.; Friedland, N.; Tang, S.; Arunachalam, P.S.; Hu, M.; Kumru, O.S.; Morris, M.K.; Fontenot, 
          J.; Shirreff, L.; Do, J.; Cheng, Y.-C.; Vasudevan, G.; Feinberg, M.B.; Villinger, F.J.; Hanson, C.; Joshi, S.B.; Volkin, D. B.; 
         Pulendran, B.; Kim, P.S.; A ferritin-based COVID-19 nanoparticle vaccine that elicits robust, durable, broad-spectrum 
         neutralizing antisera in non-human primates. Nature Communications, 17 April 2023, 14, 2149, 
         https://doi.org/10.1038/s41467-023-37417-9
Guo, X.; Zhang, J.; Han, L.; Lee, J.; Williams, S.C.; Forsberg, A.; Xu, Y.; Narehood Austin, R.; Feng, L.; Structure and mechanism 
         of the alkane-oxidizing enzyme AlkB. Nature Communications, 17 April 2023, 14, 2180,
         https://doi.org/10.1038/s41467-023-37869-z
Yang, K.; Wang, C.; Kreutzberger, A.J.B.; White, K.I.; Pfuetzner, R.A.; Esquivies, L.; Kirchhausen, T.; Brunger, A.T. Structure-
         based design of a SARS-CoV-2 Omicron-specific inhibitor. Proceedings of the National Academy of Sciences, 2023.03.20, 
         120(13), e2300360120. https://doi.org/10.1073/pnas.2300360120
Gangwar, S.P.; Yen, L.Y.; Yelshanskaya, M.V.; Sobolevsky, A.I. Positive and negative allosteric modulation of GluK2 kainate 
         receptors by BPAM344 and antiepileptic perampanel. Cell Reports, 2023.02.28, 42(2), 112124,
         https//doi.org/10.106/j.cerep.2023.112124
Fan, M.; Zhang, J.; Lee, C-L.; Zhang, J.; Feng, L. Structure and thiazide inhibition mechanism of the human Na-CI cotransporter. 
        Nature, 2023.02.15, 614, 788-793 (2023), https://doi.org/10.1038/s41586-023-05718-0
Richards, L.S.; Flores, M.D.; Zink, S.; Schibrowsky, N.A.; Sawaya, M.R.; Rodriguez, J.A. Cryo-EM Structure of a Human LECT2 
       Amyloid Fibril Reveals a Network of Polar Ladders at its Core. bioRxiv (Preprint 02.11.23) 
       https://doi.org/10.1101/2023.02.08.527771
Molodtsov, V.; Wang, C.; Firlar, E.; Kaelber, J.T.; Ebright, R.H. Structural basis of Rho-dependent transcription termination. 
        Nature 25 January 2023, 614, 367-374, https://doi.org/10.1038/s41586-022-05658-1
Shen, J; Wilbon, A.S.; Zhou, M.; Pan, Y. Mechanism of Ca2+ transport by ferroportin. eLife, 2023.01.23, 12:e82947,  
        https://doi.org/10.7554/eLife.82947

Nguyen, B.A.; Afrin, S.; Singh, V.; Ahmed, Y.; Pedretti, R.; Fernandez-Ramirez, M.D.C.; Benson, M.D.; Sawaya, M.; Singh, P.; Cao, Q.; Boyer, D.; 
        Pope, A.; Wydorski, P.; Kumar, Si.; Chhapra, F.; Eisenberg, D.; Saelices, L.; Structural polymorphism of amyloid fibrils in cardiac 
        transthyretin amyloidosis revealed by cryo-electron microscopy. bioRxiv (Preprint Posted 10.12.22) https://doi.org/10.1101/2022.06.21.496949
Li, S.; Palo, M.Z.; Pintilie, G.; Zhang, X.; Su, Z.; Kappel, K.; Chiu, W.; Zhang, K.; Das, R. Topological crossing in the misfolded tetrahymena 
         ribozyme resolved by cryo-EM. Proc national Acad Sci. 2022, 119, e2209146119. https//doi.org/10.1073/pnas.2209146119
Yu, Z.; Chen, J.; Takagi, E.; Wang, F.; Saha, B.; Liu, X.; Joubert, L.-M.; Gleason, C. E.; Jin, M.; Li, C.; Nowotny, C.; Agard, D.; Cheng, Y.;
         Pearce, D. Interactions between MTORC2 Core Subunits Rictor and MSin1 Dictate Selective and Context-Dependent 
         Phosphorylation of Substrate Kinases SGK1 and Akt. J Biol Chem 2022, 102288. https://doi.org/10.1016/j.jbc.2022.102288 
Smith, E. M.; Ferrell, S.; Tokars, V. L.; Mondragón, A. Structures of an Active Type III-A CRISPR Effector Complex. Structure 2022, 
       30 (8), 1109-1128.e6. https://doi.org/10.1016/j.str.2022.05.013 
Khant, H.; Li, Y. T.; Shankar, M.; Hecksel, C.; Mitchell, P.; Liu, Y.; Joubert, L.-M.; Zhang, C.; Dunn, L.; Schmid, M.; Hedman, B.; Chiu, W. 
         Cryo-EM Information Management System and Sample Evaluation at Stanford-SLAC Cryo-EM Center. Microsc Microanal 2022, 
         28 (S1), 1304–1305. https://doi.org/10.1017/s1431927622005359 
Rutledge, H. L.; Cook, B. D.; Nguyen, H. P. M.; HerzikJr., M. A.; Tezcan, F. A. Structures of the Nitrogenase Complex Prepared under 
        Catalytic Turnover Conditions. Science 2022, eabq7641. https://doi.org/10.1126/science.abq7641 
Li, F.; Eriksen, J.; Oses-Prieto, J.A.; Gomez, Y.K.; Xu, H.; Finer-Moore, J.; Nguyen, P.; Bowen, A.; Nelson, A.; Burlingame, A.; Grabe, M.; 
         Stroud, R.M.; Edwards, R.H. Allosteric Regulation of a Synaptic Vesicle Glutamate Transporter. BioRxiv2022, 2022.07.26.501550. 
         https://doi.org/10.1101/2022.07.26.501550 (preprint)
Kim, D. S.; Watkins, A.; Bidstrup, E.; Lee, J.; Topkar, V.; Kofman, C.; Schwarz, K. J.; Liu, Y.; Pintilie, G.; Roney, E.; Das, R.; Jewett, M. C. 
        Three-Dimensional Structure-Guided Evolution of a Ribosome with Tethered Subunits. Nat Chem Biol 2022, 1–9. 
        https://doi.org/10.1038/s41589-022-01064-w 
Fontana, P.; Dong, Y.; Pi, X.; Tong, A. B.; Hecksel, C. W.; Wang, L.; Fu, T.-M.; Bustamante, C.; Wu, H. Structure of Cytoplasmic Ring 
       of Nuclear Pore Complex by Integrative Cryo-EM and AlphaFold. Science 2022, 376 (6598), eabm9326. 
       https://doi.org/10.1126/science.abm9326 
Yelshanskaya, M. V.; Patel, D. S.; Kottke, C. M.; Kurnikova, M. G.; Sobolevsky, A. I. Opening of Glutamate Receptor Channel to 
       Subconductance Levels. Nature 2022, 605 (7908), 172–178. https://doi.org/10.1038/s41586-022-04637-w 
Yang, K.; Wang, C.; White, K. I.; Pfuetzner, R. A.; Esquivies, L.; Brunger, A. T. Structural Conservation among Variants of the SARS-CoV-2 
         Spike Postfusion Bundle. Proc National Acad Sci 2022, 119 (16), e2119467119. https://doi.org/10.1073/pnas.2119467119 
Abskharon, R.; Sawaya, M. R.; Boyer, D. R.; Cao, Q.; Nguyen, B. A.; Cascio, D.; Eisenberg, D. S. Cryo-EM Structure of RNA-Induced Tau 
         Fibrils Reveals a Small C-Terminal Core That May Nucleate Fibril Formation. Proc National Acad Sci 2022, 119 (15), e2119952119. 
         https://doi.org/10.1073/pnas.2119952119 
Fan, C.; Rees, D. C. Glutathione Binding to the Plant AtAtm3 Transporter and Implications for the Conformational Coupling 
         of ABC Transporters. Elife 2022, 11, e76140. https://doi.org/10.7554/elife.76140 
Jiang, M.; Shin, J.; Simeon, R.; Chang, J.-Y.; Meng, R.; Wang, Y.; Shinde, O.; Li, P.; Chen, Z.; Zhang, J. Structural Dynamics of Receptor 
        Recognition and PH-Induced Dissociation of Full-Length Clostridioides Difficile Toxin B. Plos Biol 2022, 20 (3), e3001589. 
        https://doi.org/10.1371/journal.pbio.3001589 
Kafai, N. M.; Williamson, L. E.; Binshtein, E.; Sukupolvi-Petty, S.; Gardner, C. L.; Liu, J.; Mackin, S.; Kim, A. S.; Kose, N.; Carnahan, 
        R. H.; Jung, A.; Droit, L.; Reed, D. S.; Handley, S. A.; Klimstra, W. B.; Crowe, J. E.; Diamond, M. S. Neutralizing Antibodies Protect 
        Mice against Venezuelan Equine Encephalitis Virus Aerosol Challenge. J Exp Med 2022, 219 (4), e20212532.
        https://doi.org/10.1084/jem.20212532 
Koo, C. W.; Tucci, F. J.; He, Y.; Rosenzweig, A. C. Recovery of Particulate Methane Monooxygenase Structure and Activity in a Lipid 
        Bilayer. Science 2022, 375 (6586), 1287–1291. https://doi.org/10.1126/science.abm3282 
Tsai, K.; Stojković, V.; Lee, D. J.; Young, I. D.; Szal, T.; Klepacki, D.; Vázquez-Laslop, N.; Mankin, A. S.; Fraser, J. S.; Fujimori, D. G. Structural Basis for 
          Context-Specific Inhibition of Translation by Oxazolidinone Antibiotics. Nat Struct Mol Biol 2022, 29 (2), 162–171.
          https://doi.org/10.1038/s41594-022-00723-9 
Zimanyi, C. M.; Kopylov, M.; Potter, C. S.; Carragher, B.; Eng, E. T. Broadening Access to CryoEM through Centralized Facilities. Trends Biochem Sci 
         2021, 47 (2), 106–116. https://doi.org/10.1016/j.tibs.2021.10.007 
Zhou, W.; Bammes, B.; Mitchell, P. G.; Betz, K.; Chiu, W. Electron Crystallography of Chiral and Non-Chiral Small Molecules. 
         Ultramicroscopy 2022, 232, 113417. https://doi.org/10.1016/j.ultramic.2021.113417 

Klykov, O.; Gangwar, S. P.; Yelshanskaya, M. V.; Yen, L.; Sobolevsky, A. I. Structure and Desensitization of AMPA Receptor Complexes with Type II 
        TARP Γ5 and GSG1L. Mol Cell 2021, 81 (23), 4771-4783.e7. https://doi.org/10.1016/j.molcel.2021.09.030 
Cogan, D. P.; Zhang, K.; Li, X.; Li, S.; Pintilie, G. D.; Roh, S.-H.; Craik, C. S.; Chiu, W.; Khosla, C. Mapping the Catalytic Conformations of an Assembly-
         Line Polyketide Synthase Module. Science 2021, 374 (6568), 729–734. https://doi.org/10.1126/science.abi8358 
Neuberger, A.; Nadezhdin, K. D.; Sobolevsky, A. I. Structural Mechanisms of TRPV6 Inhibition by Ruthenium Red and Econazole. Nat Commun 
         2021, 12 (1), 6284. https://doi.org/10.1038/s41467-021-26608-x 
Harris, J. A.; Faust, B.; Gondin, A. B.; Dämgen, M. A.; Suomivuori, C.-M.; Veldhuis, N. A.; Cheng, Y.; Dror, R. O.; Thal, D. M.; Manglik, A. 
        Selective G Protein Signaling Driven by Substance P–Neurokinin Receptor Dynamics. Nat Chem Biol 2022, 18 (1), 109–115. 
        https://doi.org/10.1038/s41589-021-00890-8 
Sheedlo, M. J.; Durie, C. L.; Chung, J. M.; Chang, L.; Roberts, J.; Swanson, M.; Lacy, D. B.; Ohi, M. D. Cryo-EM Reveals New Species-Specific Proteins 
        and Symmetry Elements in the Legionella Pneumophila Dot/Icm T4SS. Elife 2021, 10, e70427. https://doi.org/10.7554/elife.70427 
Zhang, K.; Zheludev, I. N.; Hagey, R. J.; Haslecker, R.; Hou, Y. J.; Kretsch, R.; Pintilie, G. D.; Rangan, R.; Kladwang, W.; Li, S.; Wu, M. T.-P.; Pham, E. A.; 
        Bernardin-Souibgui, C.; Baric, R. S.; Sheahan, T. P.; D’Souza, V.; Glenn, J. S.; Chiu, W.; Das, R. Cryo-EM and Antisense Targeting of the 28-KDa 
        Frameshift Stimulation Element from the SARS-CoV-2 RNA Genome. Nat Struct Mol Biol 2021, 28 (9), 747–754. 
        https://doi.org/10.1038/s41594-021-00653-y 
Hecksel, C.; Zhang, K.; Pintilie, G.; Mitchell, P.; Li, Y.-T.; Chiu, W. High Resolution Data Collection at S2C2, a National CryoEM Center. Microsc 
        Microanal 2021, 27 (S1), 1152–1154. https://doi.org/10.1017/s1431927621004359 
Eriksen, J.; Li, F.; Stroud, R. M.; Edwards, R. H. Allosteric Inhibition of a Vesicular Glutamate Transporter by an Isoform-Specific Antibody. 
        Biochemistry-us 2021, 60 (32), 2463–2470. https://doi.org/10.1021/acs.biochem.1c00375 
Hu, W.; Parkinson, C.; Zheng, H. Mechanistic Insights Revealed by YbtPQ in the Occluded State. BioRxiv 2021, 2021.06.15.448544. 
         https://doi.org/10.1101/2021.06.15.448544 (preprint)
He, Y.; Wang, Y.; Liu, B.; Helmling, C.; Sušac, L.; Cheng, R.; Zhou, Z. H.; Feigon, J. Structures of Telomerase at Several Steps of Telomere Repeat 
         Synthesis. Nature 2021, 593 (7859), 454–459. https://doi.org/10.1038/s41586-021-03529-9.
Horikoshi, N.; Hwang, S.; Gati, C.; Matsui, T.; Castillo-Orellana, C.; Raub, A. G.; Garcia, A. A.; Jabbarpour, F.; Batyuk, A.; Broweleit, J.; Xiang, X.; 
        Chiang, A.; Broweleit, R.; Vöhringer-Martinez, E.; Mochly-Rosen, D.; Wakatsuki, S. Long-Range Structural Defects by Pathogenic Mutations 
        in Most Severe Glucose-6-Phosphate Dehydrogenase Deficiency. Proc National Acad Sci 2021, 118 (4), e2022790118. 
        https://doi.org/10.1073/pnas.2022790118 
Powell, A. E.; Zhang, K.; Sanyal, M.; Tang, S.; Weidenbacher, P. A.; Li, S.; Pham, T. D.; Pak, J. E.; Chiu, W.; Kim, P. S. A Single Immunization with Spike-
         Functionalized Ferritin Vaccines Elicits Neutralizing Antibody Responses against SARS-CoV-2 in Mice. ACS Central Sci 2021, 7 (1), 183–199. 
         https://doi.org/10.1021/acscentsci.0c01405 

Zhang, K.; Li, S.; Pintilie, G.; Chmielewski, D.; Schmid, M. F.; Simmons, G.; Jin, J.; Chiu, W. A 3.4-Å Cryo-Electron Microscopy
         Structure of the Human Coronavirus Spike Trimer Computationally Derived from Vitrified NL63 Virus Particles. Qrb 
         Discov 2020, 1, e11. https://doi.org/10.1017/qrd.2020.16
Zhang, K.; Pintilie, G. D.; Li, S.; Schmid, M. F.; Chiu, W. Resolving Individual Atoms of Protein Complex by Cryo-Electron
        Microscopy. Cell Res 2020, 30 (12), 1136–1139. https://doi.org/10.1038/s41422-020-00432-2 
Roh, S.-H.; Shekhar, M.; Pintilie, G.; Chipot, C.; Wilkens, S.; Singharoy, A.; Chiu, W. Cryo-EM and MD Infer Water-Mediated
         Proton Transport and Autoinhibition Mechanisms of Vo Complex. Sci Adv 2020, 6 (41), eabb9605. 
         https://doi.org/10.1126/sciadv.abb9605 
Fromm, S. A.; Lawrence, R. E.; Hurley, J. H. Structural Mechanism for Amino Acid-Dependent Rag GTPase Nucleotide
         State Switching by SLC38A9. Nat Struct Mol Biol 2020, 27 (11), 1017–1023. https://doi.org/10.1038/s41594-020-0490-9 
Fan, C.; Kaiser, J. T.; Rees, D. C. A Structural Framework for Unidirectional Transport by a Bacterial ABC Exporter. 
         Proc National Acad Sci 2020, 117 (32), 19228–19236. https://doi.org/10.1073/pnas.2006526117
Kumar, A.; Basak, S.; Rao, S.; Gicheru, Y.; Mayer, M. L.; Sansom, M. S. P.; Chakrapani, S. Mechanisms of Activation and 
        Desensitization of Full-Length Glycine Receptor in Lipid Nanodiscs. Nat Commun 2020, 11 (1), 3752. 
        https://doi.org/10.1038/s41467-020-17364-5 
Partin, A. C.; Zhang, K.; Jeong, B.-C.; Herrell, E.; Li, S.; Chiu, W.; Nam, Y. Cryo-EM Structures of Human Drosha and DGCR8 
         in Complex with Primary MicroRNA. Mol Cell 2020, 78 (3), 411-422.e4. https://doi.org/10.1016/j.molcel.2020.02.016 
Chiu, W. Stanford-SLAC Cryo-EM Center. Acta Crystal 2020, 76 (a1), a200–a200. https://doi.org/10.1107/s0108767320098025 

Chiu, W.; Li, Y. T.; Bushnell, D.; Schmid, M. F.; Skiniotis, G.; Hedman, B. Stanford-SLAC Cryo-EM Center (S2C2). Microsc 
        Microanal 2019, 25 (S2), 2658–2659. https://doi.org/10.1017/s1431927619014028
Buffalo, C. Z.; Stürzel, C. M.; Heusinger, E.; Kmiec, D.; Kirchhoff, F.; Hurley, J. H.; Ren, X. Structural Basis for Tetherin 
       Antagonism as a Barrier to Zoonotic Lentiviral Transmission. Cell Host Microbe 2019, 26 (3), 359-368.e8. 
       https://doi.org/10.1016/j.chom.2019.08.002​

Theses

Hoppe, N.W. Adv (2023) Structural Insights into Orphan G Protein-Coupled Receptors: A Focus on GPR161 and Proton-Sensing
         GPCRs. UCSF. ProQuest ID: Hoppe_UCSF_0034D_12613. Merritt ID: ark:/13030/m57q9stg. Retreived from
          https://escholarship.org/uc/item/4n65t4w6
Rosenberg, G.M. (2023). Genetic Causes of Amyloid Fibrils and Their Structures. UCLA. ProQuest ID: Rosenberg_ucla_0031D_22088. 
         Merritt ID: ark:/13030/m5191m86. Retrieved from https://escholarship.org/uc/item/914702p
S2C2 | Stanford-SLAC CryoEM Center
2575 Sand Hill Road
Menlo Park, CA 94025
  • Contact Us

Footer Menu

  • Cryo-EM Centers Home Page
    • S2C2 Cryo-EM Home Page
    • SCSC Cryo-ET Home Page
  • QUICK LINKS FOR USERS
    • SLAC User Portal
    • CryoEM eLogBook
    • Project Review Committee
    • Unix Account Requests
    • Sample Shipping Form
    • CryoEM's Confluence Website
  • Facebook
  • Twitter
  • Instagram
  • Flickr
  • Youtube
  • LinkedIn
  • Staff portal
  • Privacy policy
  • Accessibility
  • Vulnerability disclosure
SLAC
  • SLAC home
  • Maps & directions
  • Emergency info
  • Careers

© 2025 SLAC National Accelerator Laboratory is operated by Stanford University for the U.S. Department of Energy Office of Science.

Stanford University U.S. Department of Energy
Top Top
Back to top Back to top