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学術論文

In vivo protein crystallization opens new routes in structural biology

MPS-Authors
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Nass,  Karol
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117878

Doak,  R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92822

Erk,  Benjamin
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92933

Foucar,  Lutz
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93693

Kassemeyer,  Stephan
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94117

Lomb,  Lukas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117794

Rolles,  Daniel
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95029

Rudek,  Benedikt
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95345

Shoeman,  Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://dx.doi.org/10.1038/nmeth.1859
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引用

Koopmann, R., Cupelli, K., Redecke, L., Nass, K., DePonte, D. P., White, T. A., Stellato, F., Rehders, D., Liang, M., Andreasson, J., Aquila, A., Bajt, S., Barthelmess, M., Barty, A., Bogan, M. J., Bostedt, C., Boutet, S., Bozek, J. D., Caleman, C., Coppola, N., Davidsson, J., Doak, R. B., Ekeberg, T., Epp, S. W., Erk, B., Fleckenstein, H., Foucar, L., Graafsma, H., Gumprecht, L., Hajdu, J., Hampton, C. Y., Hartmann, A., Hartmann, R., Hauser, G., Hirsemann, H., Holl, P., Hunter, M. S., Kassemeyer, S., Kirian, R. A., Lomb, L., Maia, F. R. N. C., Kimmel, N., Martin, A. V., Messerschmidt, M., Reich, C., Rolles, D., Rudek, B., Rudenko, A., Schlichting, I., Schulz, J., Seibert, M. M., Shoeman, R. L., Sierra, R. G., Soltau, H., Stern, S., Strüder, L., Timneanu, N., Ullrich, J., Wang, X., Weidenspointner, G., Weierstall, U., Williams, G. J., Wunderer, C. B., Fromme, P., Spence, J. C. H., Stehle, T., Chapman, H. N., Betzel, C., & Duszenko, M. (2012). In vivo protein crystallization opens new routes in structural biology. Nature methods, 9(3), 259-262. doi:10.1038/nmeth.1859.


引用: https://hdl.handle.net/11858/00-001M-0000-0024-1E14-3
要旨
Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X−ray crystallographic analysis. We prepared nano−sized in vivo−grown crystals of Trypanosoma brucei enzymes and applied the emerging method of free−electron laser−based serial femtosecond crystallography to record interpretable diffraction data. This combined approach will open new opportunities in structural systems biology