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198(5), 913–925 (2012). doi:10.1083/jcb.201201120
40. T. Oda, T. Abe, H. Yanagisawa, M. Kikkawa, Structure and function of outer dynein arm
intermediate and light chain complex. Mol. Biol. Cell (2016). doi:10.1091/mbc.E15-10-0723
41. J. Lin, W. Yin, M.C. Smith, K. Song, M.W. Leigh, M.A. Zariwala, M.R. Knowles, L.E.
Ostrowski, D. Nicastro, Cryo-electron tomography reveals ciliary defects underlying human
RSPH1 primary ciliary dyskinesia. Nat. Commun. 5, 5727 (2014). doi:10.1038/ncomms6727
42. M. Beck, V. Lucic, F. Forster, W. Baumeister, O. Medalia, Snapshots of nuclear pore
complexes in action captured by cryo-electron tomography. Nature 449(7162), 611–615
(2007). doi:10.1038/nature06170
43. M. Beck, F. Forster, M. Ecke, J.M. Plitzko, F. Melchior, G. Gerisch, W. Baumeister, O.
Medalia, Nuclear pore complex structure and dynamics revealed by cryoelectron tomography.
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44. A. von Appen, J. Kosinski, L. Sparks, A. Ori, A.L. DiGuilio, B. Vollmer, M.T. Mackmull, N.
Banterle, L. Parca, P. Kastritis, K. Buczak, S. Mosalaganti, W. Hagen, A. Andres-Pons, E.A.
Lemke, P. Bork, W. Antonin, J.S. Glavy, K.H. Bui, M. Beck, In situ structural analysis of the
human nuclear pore complex. Nature 526(7571), 140–143 (2015). doi:10.1038/nature15381
45. M. Eibauer, M. Pellanda, Y. Turgay, A. Dubrovsky, A. Wild, O. Medalia, Structure and
gating of the nuclear pore complex. Nat. Commun. 6, 7532 (2015). doi:10.1038/ncomms8532
46. K.H. Bui, A. von Appen, A.L. DiGuilio, A. Ori, L. Sparks, M.T. Mackmull, T. Bock, W.
Hagen, A. Andres-Pons, J.S. Glavy, M. Beck, Integrated structural analysis of the human
nuclear pore complex scaffold. Cell 155(6), 1233–1243 (2013). doi:10.1016/j.cell.2013.10.
055
47. T. Maimon, N. Elad, I. Dahan, O. Medalia, The human nuclear pore complex as revealed by
cryo-electron tomography. Structure 20(6), 998–1006 (2012). doi:10.1016/j.str.2012.03.025
48. M. Faini, S. Prinz, R. Beck, M. Schorb, J.D. Riches, K. Bacia, B. Brugger, F.T. Wieland, J.A.
Briggs, The structures of COPI-coated vesicles reveal alternate coatomer conformations and
interactions. Science 336(6087), 1451–1454 (2012). doi:10.1126/science.1221443
49. S.O. Dodonova, P. Diestelkoetter-Bachert, A. von Appen, W.J. Hagen, R. Beck, M. Beck, F.
Wieland, J.A. Briggs, VESICULAR TRANSPORT. A structure of the COPI coat and the role
of coat proteins in membrane vesicle assembly. Science 349(6244), 195–198 (2015). doi:10.
1126/science.aab1121
50. G. Zanetti, S. Prinz, S. Daum, A. Meister, R. Schekman, K. Bacia, J.A. Briggs, The structure
of the COPII transport-vesicle coat assembled on membranes. Elife 2, e00951 (2013). doi:10.
7554/eLife.00951
51. F.K. Schur, W.J. Hagen, M. Rumlova, T. Ruml, B. Muller, H.G. Krausslich, J.A. Briggs,
Structure of the immature HIV-1 capsid in intact virus particles at 8.8 A resolution. Nature
517(7535), 505–508 (2015). doi:10.1038/nature13838
52. F.K. Schur, R.A. Dick, W.J. Hagen, V.M. Vogt, J.A. Briggs, The structure of immature
virus-like rous sarcoma virus gag particles reveals a structural role for the p10 domain in
assembly. J. Virol. 89(20), 10294–10302 (2015). doi:10.1128/JVI.01502-15
53. G.E. Murphy, J.R. Leadbetter, G.J. Jensen, In situ structure of the complete Treponema
primitia flagellar motor. Nature 442(7106), 1062–1064 (2006). doi:10.1038/nature05015
54. S. Chen, M. Beeby, G.E. Murphy, J.R. Leadbetter, D.R. Hendrixson, A. Briegel, Z. Li, J. Shi,
E.I. Tocheva, A. Muller, M.J. Dobro, G.J. Jensen, Structural diversity of bacterial flagellar
motors. EMBO J. 30(14), 2972–2981 (2011). doi:10.1038/emboj.2011.186
55. X. Zhao, K. Zhang, T. Boquoi, B. Hu, M.A. Motaleb, K.A. Miller, M.E. James, N.W. Charon,
M.D. Manson, S.J. Norris, C. Li, J. Liu, Cryoelectron tomography reveals the sequential
assembly of bacterial flagella in Borrelia burgdorferi. Proc. Natl. Acad. Sci. U.S.A. 110(35),
14390–14395 (2013). doi:10.1073/pnas.1308306110
258
S. Pfeffer and F. Förster