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1. R. J. Southworth-Davies, M. A. Medina, I. Carmichael, and E. F. Garman, “ Observation of decreased radiation damage at higher dose rates in room temperature protein crystallography,” Structure 15, 15311541 (2007).
2. J. M. Holton and K. A. Frankel, “ The minimum crystal size needed for a complete diffraction data set,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 66, 393408 (2010).
3. R. Henderson, “ Cryoprotection of protein crystals against radiation damage in electron and X-ray diffraction,” Proc. R. Soc. London, Ser. B 241, 68 (1990).
4. E. F. Garman and T. R. Schneider, “ Macromolecular Cryocrystallography,” J. Appl. Crystallogr. 30, 211237 (1997).
5. R. M. Bill, P. J. Henderson, S. Iwata, E. R. Kunji, H. Michel, R. Neutze, S. Newstead, B. Poolman, C. G. Tate, and H. Vogel, “ Overcoming barriers to membrane protein structure determination,” Nat. Biotechnol. 29, 335340 (2011).
6. A. McPherson and J. A. Gavira, “ Introduction to protein crystallization,” Acta Crystallogr., Sect. F: Struct. Biol. Commun. 70, 220 (2014).
7. M. Weselak, M. G. Patch, T. L. Selby, G. Knebel, and R. C. Stevens, “ Robotics for automated crystal formation and analysis,” Methods Enzymol. 368, 4576 (2003).
8. J. P. K. Doye and W. C. K. Poon, “ Protein crystallization in vivo,” Curr. Opin. Colloid Interface Sci. 11, 4046 (2006).
9. A. McPherson, Crystallization of Biological Macromolecules ( Cold Spring Harbor Laboratory Press, 1999).
10. P. M. Colman, E. Suzuki, and A. Van Donkelaar, “ The structure of cucurbitin: Subunit symmetry and organization in situ,” Eur. J. Biochem. 103, 585588 (1980).
11. K. Müntz, “ Deposition of storage proteins,” Plant Mol. Biol. 38, 7799 (1998).
12. G. Dodson and D. Steiner, “ The role of assembly in insulin's biosynthesis,” Curr. Opin. Struct. Biol. 8, 189194 (1998).
13. M. Veenhuis, J. A. Kiel, and I. J. van der Klei, “ Peroxisome assembly in yeast,” Microsc. Res. Tech. 61, 139150 (2003).
14. H. Höfte and H. R. Whiteley, “ Insecticidal crystal proteins of Bacillus thuringiensis,” Microbiol. Rev. 53, 242255 (1989).
15. G. F. Rohrmann, “ Polyhedrin structure,” J. Gen. Virol. 67, 14991513 (1986).
16. F. Coulibaly, E. Chiu, K. Ikeda, S. Gutmann, P. W. Haebel, C. Schulze-Briese, H. Mori, and P. Metcalf, “ The molecular organization of cypovirus polyhedra,” Nature 446, 97101 (2007).
17. G. Y. Fan, F. Maldonado, Y. Zhang, R. Kincaid, M. H. Ellisman, and L. N. Gastinel, “ In vivo calcineurin crystals formed using the baculovirus expression system,” Microsc. Res. Tech. 34, 7786 (1996).<77::AID-JEMT11>3.0.CO;2-M
18. H. Hasegawa, J. Wendling, F. He, E. Trilisky, R. Stevenson, H. Franey, F. Kinderman, G. Li, D. M. Piedmonte, T. Osslund, M. Shen, and R. R. Ketchem, “ In vivo crystallization of human IgG in the endoplasmic reticulum of engineered Chinese hamster ovary (CHO) cells,” J. Biol. Chem. 286, 1991719931 (2011).
19. H. Hasegawa, C. Forte, I. Barber, S. Turnbaugh, J. Stoops, M. Shen, and A. C. Lim, “ Modulation of in vivo IgG crystallization in the secretory pathway by heavy chain isotype class switching and N-linked glycosylation,” Biochim. Biophys. Acta 1843, 13251338 (2014).
20. F. X. Gallat, N. Matsugaki, N. P. Coussens, K. J. Yagi, M. Boudes, T. Higashi, D. Tsuji, Y. Tatano, M. Suzuki, E. Mizohata, K. Tono, Y. Joti, T. Kameshima, J. Park, C. Song, T. Hatsui, M. Yabashi, E. Nango, K. Itoh, F. Coulibaly, S. Tobe, S. Ramaswamy, B. Stay, S. Iwata, and L. M. Chavas, “ In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology?,” Philos. Trans. R. Soc. London, Ser. B: Biol. Sci. 369, 20130497 (2014).
21. D. Axford, X. Ji, D. I. Stuart, and G. Sutton, “ In cellulo structure determination of a novel cypovirus polyhedrin,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 70, 14351441 (2014).
22. R. Neutze, R. Wouts, D. van der Spoel, E. Weckert, and J. Hajdu, “ Potential for biomolecular imaging with femtosecond X-ray pulses,” Nature 406, 752757 (2000).
23. H. N. Chapman, P. Fromme, A. Barty, T. A. White, R. A. Kirian, A. Aquila, M. S. Hunter, J. Schulz, D. P. DePonte, U. Weierstall, R. B. Doak, F. R. Maia, A. V. Martin, I. Schlichting, L. Lomb, N. Coppola, R. L. Shoeman, S. W. Epp, R. Hartmann, D. Rolles, A. Rudenko, L. Foucar, N. Kimmel, G. Weidenspointner, P. Holl, M. Liang, M. Barthelmess, C. Caleman, S. Boutet, M. J. Bogan, J. Krzywinski, C. Bostedt, S. Bajt, L. Gumprecht, B. Rudek, B. Erk, C. Schmidt, A. Hömke, C. Reich, D. Pietschner, L. Strüder, G. Hauser, H. Gorke, J. Ullrich, S. Herrmann, G. Schaller, F. Schopper, H. Soltau, K. U. Kühnel, M. Messerschmidt, J. D. Bozek, S. P. Hau-Riege, M. Frank, C. Y. Hampton, R. G. Sierra, D. Starodub, G. J. Williams, J. Hajdu, N. Timneanu, M. M. Seibert, J. Andreasson, A. Rocker, O. Jönsson, M. Svenda, S. Stern, K. Nass, R. Andritschke, C. D. Schröter, F. Krasniqi, M. Bott, K. E. Schmidt, X. Wang, I. Grotjohann, J. M. Holton, T. R. Barends, R. Neutze, S. Marchesini, R. Fromme, S. Schorb, D. Rupp, M. Adolph, T. Gorkhover, I. Andersson, H. Hirsemann, G. Potdevin, H. Graafsma, B. Nilsson, and J. C. Spence, “ Femtosecond X-ray protein nanocrystallography,” Nature 470, 7377 (2011).
24. S. Boutet, L. Lomb, G. J. Williams, T. R. Barends, A. Aquila, R. B. Doak, U. Weierstall, D. P. DePonte, J. Steinbrener, R. L. Shoeman, M. Messerschmidt, A. Barty, T. A. White, S. Kassemeyer, R. A. Kirian, M. M. Seibert, P. A. Montanez, C. Kenney, R. Herbst, P. Hart, J. Pines, G. Haller, S. M. Gruner, H. T. Philipp, M. W. Tate, M. Hromalik, L. J. Koerner, N. van Bakel, J. Morse, W. Ghonsalves, D. Arnlund, M. J. Bogan, C. Caleman, R. Fromme, C. Y. Hampton, M. S. Hunter, L. C. Johansson, G. Katona, C. Kupitz, M. Liang, A. V. Martin, K. Nass, L. Redecke, F. Stellato, N. Timneanu, D. Wang, N. A. Zatsepin, D. Schafer, J. Defever, R. Neutze, P. Fromme, J. C. Spence, H. N. Chapman, and I. Schlichting, “ High-resolution protein structure determination by serial femtosecond crystallography,” Science 337, 362364 (2012).
25. T. A. White, R. A. Kirian, A. V. Martin, A. Aquila, K. Nass, A. Barty, and H. N. Chapman, “ CrystFEL: A software suite for snapshot serial crystallography,” J. Appl. Crystallogr. 45, 335341 (2012).
26. A. Barty, R. A. Kirian, F. R. N. C. Maia, M. Hantke, C. H. Yoon, T. A. White, and H. N. Chapman, “ Cheetah: Software for high-throughput reduction and analysis of serial femtosecond X-ray diffraction data,” J. Appl. Crystallogr. 47, 11181131 (2014).
27. R. A. Kirian, T. A. White, J. M. Holton, H. N. Chapman, P. Fromme, A. Barty, L. Lomb, A. Aquila, F. R. Maia, A. V. Martin, R. Fromme, X. Wang, M. S. Hunter, K. E. Schmidt, and J. C. Spence, “ Structure-factor analysis of femtosecond microdiffraction patterns from protein nanocrystals,” Acta Crystallogr., Sect. A: Found. Crystallogr. 67, 131140 (2011).
28. D. P. DePonte, U. Weierstall, K. Schmidt, J. Warner, D. Starodub, J. C. H. Spence, and R. B. Doak, “ Gas dynamic virtual nozzle for generation of microscopic droplet streams,” J. Phys. D: Appl. Phys. 41, 195505 (2008).
29. U. Weierstall, D. James, C. Wang, T. A. White, D. Wang, W. Liu, J. C. Spence, R. Bruce Doak, G. Nelson, P. Fromme, R. Fromme, I. Grotjohann, C. Kupitz, N. A. Zatsepin, H. Liu, S. Basu, D. Wacker, G. W. Han, V. Katritch, S. Boutet, M. Messerschmidt, G. J. Williams, J. E. Koglin, M. Seibert, M. Klinker, C. Gati, R. L. Shoeman, A. Barty, H. N. Chapman, R. A. Kirian, K. R. Beyerlein, R. C. Stevens, D. Li, S. T. Shah, N. Howe, M. Caffrey, and V. Cherezov, “ Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography,” Nat. Commun. 5, 3309 (2014).
30. L. Redecke, K. Nass, D. P. DePonte, T. A. White, D. Rehders, A. Barty, F. Stellato, M. Liang, T. R. Barends, S. Boutet, G. J. Williams, M. Messerschmidt, M. M. Seibert, A. Aquila, D. Arnlund, S. Bajt, T. Barth, M. J. Bogan, C. Caleman, T. C. Chao, R. B. Doak, H. Fleckenstein, M. Frank, R. Fromme, L. Galli, I. Grotjohann, M. S. Hunter, L. C. Johansson, S. Kassemeyer, G. Katona, R. A. Kirian, R. Koopmann, C. Kupitz, L. Lomb, A. V. Martin, S. Mogk, R. Neutze, R. L. Shoeman, J. Steinbrener, N. Timneanu, D. Wang, U. Weierstall, N. A. Zatsepin, J. C. Spence, P. Fromme, I. Schlichting, M. Duszenko, C. Betzel, and H. N. Chapman, “ Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser,” Science 339, 227230 (2013).
31. J. Kern, R. Alonso-Mori, R. Tran, J. Hattne, R. J. Gildea, N. Echols, C. Glöckner, J. Hellmich, H. Laksmono, R. G. Sierra, B. Lassalle-Kaiser, S. Koroidov, A. Lampe, G. Han, S. Gul, D. Difiore, D. Milathianaki, A. R. Fry, A. Miahnahri, D. W. Schafer, M. Messerschmidt, M. M. Seibert, J. E. Koglin, D. Sokaras, T. C. Weng, J. Sellberg, M. J. Latimer, R. W. Grosse-Kunstleve, P. H. Zwart, W. E. White, P. Glatzel, P. D. Adams, M. J. Bogan, G. J. Williams, S. Boutet, J. Messinger, A. Zouni, N. K. Sauter, V. K. Yachandra, U. Bergmann, and J. Yano, “ Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature,” Science 340, 491495 (2013).
32. T. R. Barends, L. Foucar, R. L. Shoeman, S. Bari, S. W. Epp, R. Hartmann, G. Hauser, M. Huth, C. Kieser, L. Lomb, K. Motomura, K. Nagaya, C. Schmidt, R. Strecker, D. Anielski, R. Boll, B. Erk, H. Fukuzawa, E. Hartmann, T. Hatsui, P. Holl, Y. Inubushi, T. Ishikawa, S. Kassemeyer, C. Kaiser, F. Koeck, N. Kunishima, M. Kurka, D. Rolles, B. Rudek, A. Rudenko, T. Sato, C. D. Schroeter, H. Soltau, L. Strueder, T. Tanaka, T. Togashi, K. Tono, J. Ullrich, S. Yase, S. I. Wada, M. Yao, M. Yabashi, K. Ueda, and I. Schlichting, “ Anomalous signal from S atoms in protein crystallographic data from an X-ray free-electron laser,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 69, 838842 (2013).
33. T. R. Barends, L. Foucar, S. Botha, R. B. Doak, R. L. Shoeman, K. Nass, J. E. Koglin, G. J. Williams, S. Boutet, M. Messerschmidt, and I. Schlichting, “ De novo protein crystal structure determination from X-ray free-electron laser data,” Nature 505, 244247 (2014).
34. M. R. Sawaya, D. Cascio, M. Gingery, J. Rodriguez, L. Goldschmidt, J. P. Colletier, M. M. Messerschmidt, S. Boutet, J. E. Koglin, G. J. Williams, A. S. Brewster, K. Nass, J. Hattne, S. Botha, R. B. Doak, R. L. Shoeman, D. P. DePonte, H. W. Park, B. A. Federici, N. K. Sauter, I. Schlichting, and D. S. Eisenberg, “ Protein crystal structure obtained at 2.9 Å resolution from injecting bacterial cells into an X-ray free-electron laser beam,” Proc. Natl. Acad. Sci. U.S.A. 111, 1276912774 (2014).
35. C. Gati, G. Bourenkov, M. Klinge, D. Rehders, F. Stellato, D. Oberthür, O. Yefanov, B. P. Sommer, S. Mogk, M. Duszenko, C. Betzel, T. R. Schneider, H. N. Chapman, and L. Redecke, “ Serial crystallography on in vivo grown microcrystals using synchrotron radiation,” IUCrJ 1, 8794 (2014).
36. F. Coulibaly, E. Chiu, S. Gutmann, C. Rajendran, P. W. Haebel, K. Ikeda, H. Mori, V. K. Ward, C. Schulze-Briese, and P. Metcalf, “ The atomic structure of baculovirus polyhedra reveals the independent emergence of infectious crystals in DNA and RNA viruses,” Proc. Natl. Acad. Sci. U.S.A. 106, 2220522210 (2009).
37. X. Ji, G. Sutton, G. Evans, D. Axford, R. Owen, and D. I. Stuart, “ How baculovirus polyhedra fit square pegs into round holes to robustly package viruses,” EMBO J. 29, 505514 (2010).
38. R. Koopmann, K. Cupelli, L. Redecke, K. Nass, D. P. Deponte, T. A. White, F. Stellato, D. Rehders, M. Liang, J. Andreasson, A. Aquila, S. Bajt, M. Barthelmess, A. Barty, M. J. Bogan, C. Bostedt, S. Boutet, J. D. Bozek, C. Caleman, N. Coppola, J. Davidsson, R. B. Doak, T. Ekeberg, S. W. Epp, B. Erk, H. Fleckenstein, L. Foucar, H. Graafsma, L. Gumprecht, J. Hajdu, C. Y. Hampton, A. Hartmann, R. Hartmann, G. Hauser, H. Hirsemann, P. Holl, M. S. Hunter, S. Kassemeyer, R. A. Kirian, L. Lomb, F. R. Maia, N. Kimmel, A. V. Martin, M. Messerschmidt, C. Reich, D. Rolles, B. Rudek, A. Rudenko, I. Schlichting, J. Schulz, M. M. Seibert, R. L. Shoeman, R. G. Sierra, H. Soltau, S. Stern, L. Strüder, N. Timneanu, J. Ullrich, X. Wang, G. Weidenspointner, U. Weierstall, G. J. Williams, C. B. Wunderer, P. Fromme, J. C. Spence, T. Stehle, H. N. Chapman, C. Betzel, and M. Duszenko, “ In vivo protein crystallization opens new routes in structural biology,” Nat. Methods 9, 259262 (2012).
39. A. Brandariz-Nuñez, R. Menaya-Vargas, J. Benavente, and J. A. Martínez-Costas, “ Versatile molecular tagging method for targeting proteins to avian reovirus muNS inclusions. Use in protein immobilization and purification,” PLoS One 5, e13961 (2010).
40. A. Brandariz-Nuñez, R. Menaya-Vargas, J. Benavente, and J. Martínez-Costas, “ Avian reovirus NS protein forms homo-oligomeric inclusions in a microtubule-independent fashion, which involves specific regions of its C-terminal domain,” J. Virol. 84, 42894301 (2010).
41. S. Ally, A. G. Larson, K. Barlan, S. E. Rice, and V. I. Gelfand, “ Opposite-polarity motors activate one another to trigger cargo transport in live cells,” J. Cell Biol. 187, 10711082 (2009).
42. N. Zurek, L. Sparks, and G. Voeltz, “ Reticulon short hairpin transmembrane domains are used to shape ER tubules,” Traffic 12, 2841 (2011).
43. J. A. Steinkamp, R. C. Habbersett, and C. C. Stewart, “ A modular detector for flow cytometric multicolor fluorescence measurements,” Cytometry 8, 353365 (1987).
44. I. Majoul, L. Gao, E. Betzig, D. Onichtchouk, E. Butkevich, Y. Kozlov, F. Bukauskas, M. L. V. Bennett, J. Lippincott-Schwartz, and R. Duden, “ Fast structural responses of gap junction membrane domains to AB5 toxins,” Proc. Natl. Acad. Sci. U.S.A. 110, E41254133 (2013).
45. F. F. Craig, A. C. Simmonds, D. Watmore, F. McCapra, and M. R. White, “ Membrane-permeable luciferin esters for assay of firefly luciferase in live intact cells,” Biochem. J. 276, 637641 (1991).
46. I. Majoul, M. Straub, S. W. Hell, R. Duden, and H. D. Söling, “ KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: Measurements in living cells using FRET,” Dev. Cell 1, 139153 (2001).
47. R. C. Jones, “ Avian reovirus infections,” Rev. Sci. Tech. 19, 614625 (2000).
48. L. Pinto da Silva and J. C. Esteves da Silva, “ Firefly chemiluminescence and bioluminescence: Efficient generation of excited states,” ChemPhysChem 13, 22572262 (2012).
49. T. Nakatsu, S. Ichiyama, J. Hiratake, A. Saldanha, N. Kobashi, K. Sakata, and H. Kato, “ Structural basis for the spectral difference in luciferase bioluminescence,” Nature 440, 372376 (2006).
50. G. A. Keller, S. Gould, M. Deluca, and S. Subramani, “ Firefly luciferase is targeted to peroxisomes in mammalian cells,” Proc. Natl. Acad. Sci. U.S.A. 84, 32643268 (1987).
51. G. Lametschwandtner, C. Brocard, M. Fransen, P. Van Veldhoven, J. Berger, and A. Hartig, “ The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it,” J. Biol. Chem. 273, 3363533643 (1998).
52. M. Schrader and H. D. Fahimi, “ The peroxisome: still a mysterious organelle,” Histochem. Cell Biol. 129, 421440 (2008).
53. F. Fan and K. V. Wood, “ Bioluminescent assays for high-throughput screening,” Assay Drug Dev. Technol. 5, 127136 (2007).
54. T. F. Massoud, R. Paulmurugan, A. De, P. Ray, and S. S. Gambhir, “ Reporter gene imaging of protein-protein interactions in living subjects,” Curr. Opin. Biotechnol. 18, 3137 (2007).
55. A. Lundin, “ Optimization of the firefly luciferase reaction for analytical purposes,” Adv. Biochem. Eng. Biotechnol. 145, 3162 (2014).
56. E. Conti, L. F. Lloyd, J. Akins, N. P. Franks, and P. Brick, “ Crystallization and preliminary diffraction studies of firefly luciferase from Photinus pyralis,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 52, 876878 (1996).
57. D. S. Auld, S. Lovell, N. Thorne, W. A. Lea, D. J. Maloney, M. Shen, G. Rai, K. P. Battaile, C. J. Thomas, A. Simeonov, R. P. Hanzlik, and J. Inglese, “ Molecular basis for the high-affinity binding and stabilization of firefly luciferase by PTC124,” Proc. Natl. Acad. Sci. U.S.A. 107, 48784883 (2010).
58. K. Anduleit, G. Sutton, J. M. Diprose, P. P. Mertens, J. M. Grimes, and D. I. Stuart, “ Crystal lattice as biological phenotype for insect viruses,” Protein Sci. 14, 27412743 (2005).
59. H. Wang, E. Wei, A. D. Quiroga, X. Sun, N. Touret, and R. Lehner, “ Altered lipid droplet dynamics in hepatocytes lacking triacylglycerol hydrolase expression,” Mol. Biol. Cell 21, 19912000 (2010).
60.See supplementary material at for localization data of in vivo firefly luciferase crystals (see Fig. S1), images of virus-free vs. baculovirus induced in vivo crystallization of luciferase (see Fig. S2), images and movie of bioluminescence induced by enzymatically active soluble firefly luciferase within living cells (see Fig. S3 and movie S3), images of GFP-μNS and luciferase crystals grown within the same cell (see Fig. S4), and the stability analysis of isolated GFP-μNS crystals preliminary to x-ray diffraction experiments (see Fig. S5).[Supplementary Material]
61. T. Ohkawa, L. E. Volkman, and M. D. Welch, “ Actin-based motility drives baculovirus transit to the nucleus and cell surface,” J. Cell Biol. 190, 187195 (2010).
62. J. C. Spence, “ Approaches to time-resolved diffraction using an XFEL,” Faraday Discuss. 171, 429438 (2014).
63. R. Neutze and K. Moffat, “ Time-resolved structural studies at synchrotrons and X-ray free electron lasers: Opportunities and challenges,” Curr. Opin. Struct. Biol. 22, 651659 (2012).
64. H. Mori, R. Ito, H. Nakazawa, M. Sumida, F. Matsubara, and Y. Minobe, “ Expression of Bombyx mori cytoplasmic polyhedrosis virus polyhedrin in insect cells by using a baculovirus expression vector, and its assembly into polyhedra,” J. Gen. Virol. 74, 99102 (1993).
65. F. Stellato, D. Oberthür, M. Liang, R. Bean, C. Gati, O. Yefanov, A. Barty, A. Burkhardt, P. Fischer, L. Galli, R. A. Kirian, J. Meyer, S. Panneerselvam, C. H. Yoon, F. Chervinskii, E. Speller, T. A. White, C. Betzel, A. Meents, and H. N. Chapman, “ Room-temperature macromolecular serial crystallography using synchrotron radiation,” IUCrJ 1, 204212 (2014).
66. M. S. Hunter, B. Segelke, M. Messerschmidt, G. J. Williams, N. A. Zatsepin, A. Barty, W. H. Benner, D. B. Carlson, M. Coleman, A. Graf, S. P. Hau-Riege, T. Pardini, M. M. Seibert, J. Evans, S. Boutet, and M. Frank, “ Fixed-target protein serial microcrystallography with an x-ray free electron laser,” Sci. Rep. 4, 6026 (2014).

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X-ray crystallography requires sufficiently large crystals to obtain structural insights at atomic resolution, routinely obtained by time-consuming screening. Recently, successful data collection was reported from protein microcrystals grown within living cells using highly brilliant free-electron laser and third-generation synchrotron radiation. Here, we analyzed crystal growth of firefly luciferase and Green Fluorescent Protein-tagged reovirus μNS by live-cell imaging, showing that dimensions of living cells did not limit crystal size. The crystallization process is highly dynamic and occurs in different cellular compartments. protein crystallization offers exciting new possibilities for proteins that do not form crystals .


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