Single-particle cryo-EM-How did it get here and where will it go

Science

Volumn 361, Issue 6405, 2018, Pages 876-880

  Cheng, Yifan ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ELECTRON MICROSCOPY; REVIEW; ANIMAL; CHEMISTRY; CRYOELECTRON MICROSCOPY; HUMAN; PROCEDURES; SINGLE MOLECULE IMAGING; TRENDS; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

CATALASE; TRANSIENT RECEPTOR POTENTIAL CHANNEL;

ANIMALS; CATALASE; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY, X-RAY; HUMANS; SINGLE MOLECULE IMAGING; TRANSIENT RECEPTOR POTENTIAL CHANNELS;

EID: 85055666132     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aat4346     Document Type: Review

References (66)

1. R. P. Feynman, in Feynman and Computation, A. J. G. Hey, Ed. (Perseus Books Cambridge, 1999), pp. 63-76.
2. Y. Shi, Cell 159, 995-1014 (2014).
3. N. Jones, Nature 505, 602-603 (2014).
4. Y. Kang et al., Nature 523, 561-567 (2015).
5. J. Frank, Ultramicroscopy 1, 159-162 (1975).
6. J. Dubochet et al., Q. Rev. Biophys. 21, 129-228 (1988).
7. D. J. De Rosier, A. Klug, Nature 217, 130-134 (1968).
8. K. A. Taylor, R. M. Glaeser, Science 186, 1036-1037 (1974).
9. K. A. Taylor, R. M. Glaeser, J. Struct. Biol. 163, 214-223 (2008).
10. J. Dubochet, J. J. Chang, R. Freeman, J. Lepault, A. W. McDowall, Ultramicroscopy 10, 55-61 (1982).
11. M. Adrian, J. Dubochet, J. Lepault, A. W. McDowall, Nature 308, 32-36 (1984).
12. H. Stark, F. Zemlin, C. Boettcher, Ultramicroscopy 63, 75-79 (1996).
13. Y. Fujiyoshi, Adv. Biophys. 35, 25-80 (1998).
14. P. N. Unwin, R. Henderson, J. Mol. Biol. 94, 425-440 (1975).
15. R. Henderson, P. N. Unwin, Nature 257, 28-32 (1975).
16. R. Henderson et al., J. Mol. Biol. 213, 899-929 (1990).
17. W. Kühlbrandt, D. N. Wang, Y. Fujiyoshi, Nature 367, 614-621 (1994).
18. K. Murata et al., Nature 407, 599-605 (2000).
19. E. Nogales, S. G. Wolf, K. H. Downing, Nature 391, 199-203 (1998).
20. T. Gonen et al., Nature 438, 633-638 (2005).
21. J. Frank, W. Goldfarb, D. Eisenberg, T. S. Baker, Ultramicroscopy 3, 283-290 (1978).
22. M. Radermacher, T. Wagenknecht, A. Verschoor, J. Frank, EMBO J. 6, 1107-1114 (1987).
23. Y. Cheng, N. Grigorieff, P. A. Penczek, T. Walz, Cell 161, 438-449 (2015).
24. R. Fernandez-Leiro, S. H. Scheres, Nature 537, 339-346 (2016).
25. R. H. Wade, Ultramicroscopy 46, 145-156 (1992).
26. S. Srivastava, A. Verschoor, M. Radermacher, R. Grassucci, J. Frank, J. Mol. Biol. 245, 461-466 (1995).
27. M. Radermacher et al., J. Cell Biol. 127, 411-423 (1994).
28. R. Henderson, Q. Rev. Biophys. 28, 171-193 (1995).
29. G. McMullan, A. R. Faruqi, R. Henderson, Methods Enzymol. 579, 1-17 (2016).
30. X. C. Bai, I. S. Fernandez, G. McMullan, S. H. Scheres, eLife 2, e00461 (2013).
31. X. Li et al., Nat. Methods 10, 584-590 (2013).
32. Y. Cheng, Cell 161, 450-457 (2015).
33. B. Böttcher, S. A. Wynne, R. A. Crowther, Nature 386, 88-91 (1997).
34. S. J. Ludtke, W. Chiu, J. Struct. Biol. 144, 73-78 (2003).
35. X. Zhang, L. Jin, Q. Fang, W. H. Hui, Z. H. Zhou, Cell 141, 472-482 (2010).
36. P. Mooney, Methods Cell Biol. 79, 661-719 (2007).
37. E. Samei, M. J. Flynn, D. A. Reimann, Med. Phys. 25, 102-113 (1998).
38. C. Suloway et al., J. Struct. Biol. 151, 41-60 (2005).
39. A. F. Brilot et al., J. Struct. Biol. 177, 630-637 (2012).
40. S. H. Scheres, eLife 3, e03665 (2014).
41. T. Grant, N. Grigorieff, eLife 4, e06980 (2015).
42. F. J. Sigworth, J. Struct. Biol. 122, 328-339 (1998).
43. S. H. Scheres, J. Mol. Biol. 415, 406-418 (2012).
44. S. H. Scheres, J. Struct. Biol. 180, 519-530 (2012).
45. D. E. Clapham, Nature 426, 517-524 (2003).
46. D. Julius, Annu. Rev. Cell Dev. Biol. 29, 355-384 (2013).
47. M. M. Moran, Annu. Rev. Pharmacol. Toxicol. 58, 309-330 (2018).
48. M. Li, Y. Yu, J. Yang, Adv. Exp. Med. Biol. 704, 1-23 (2011).
49. M. Liao, E. Cao, D. Julius, Y. Cheng, Nature 504, 107-112 (2013).
50. E. Cao, M. Liao, Y. Cheng, D. Julius, Nature 504, 113-118 (2013).
51. G. C. Lander et al., Nature 482, 186-191 (2012).
52. W. P. Galej, T. H. Nguyen, A. J. Newman, K. Nagai, Curr. Opin. Struct. Biol. 25, 57-66 (2014).
53. M. D. Ohi, L. Ren, J. S. Wall, K. L. Gould, T. Walz, Proc. Natl. Acad. Sci. U.S.A. 104, 3195-3200 (2007).
54. S. M. Fica, K. Nagai, Nat. Struct. Mol. Biol. 24, 791-799 (2017).
55. Y. Shi, Nat. Rev. Mol. Cell Biol. 18, 655-670 (2017).
56. R. Danev, B. Buijsse, M. Khoshouei, J. M. Plitzko, W. Baumeister, Proc. Natl. Acad. Sci. U.S.A. 111, 15635-15640 (2014).
57. M. Khoshouei, R. Danev, J. M. Plitzko, W. Baumeister, J. Mol. Biol. 429, 2611-2618 (2017).
58. V. P. Dandey et al., J. Struct. Biol. 202, 161-169 (2018).
59. S. Kaledhonkar, Z. Fu, H. White, J. Frank, Methods Mol. Biol. 1764, 59-71 (2018).
60. X. Li, S. Q. Zheng, K. Egami, D. A. Agard, Y. Cheng, J. Struct. Biol. 184, 251-260 (2013).
61. C. E. Paulsen, J. P. Armache, Y. Gao, Y. Cheng, D. Julius, Nature 520, 511-517 (2015).
62. H. E. Autzen et al., Science 359, 228-232 (2018).
63. D. Vinayagam et al., eLife 7, e36615 (2018).
64. P. Jin et al., Nature 547, 118-122 (2017).
65. P. S. Shen et al., Cell 167, 763-773.e11 (2016).
66. Q. Chen et al., Nature 550, 415-418 (2017).