In vivo protein crystallization opens new routes in structural biology

Koopmann, Rudolf; Cupelli, Karolina; Redecke, Lars; Nass, Karol; DePonte, Daniel P; White, Thomas A; Stellato, Francesco; Rehders, Dirk; Liang, Mengning; Andreasson, Jakob; Aquila, Andrew; Bajt, Sasa; Barthelmess, Miriam; Barty, Anton; Bogan, Michael J; Bostedt, Christoph; Boutet, Sébastien; Bozek, John D; Caleman, Carl; Coppola, Nicola; Davidsson, Jan; Doak, R Bruce; Ekeberg, Tomas; Epp, S. W.; Erk, Benjamin; Fleckenstein, Holger; Foucar, Lutz; Graafsma, Heinz; Gumprecht, Lars; Hajdu, Janos; Hampton, Christina Y; Hartmann, Andreas; Hartmann, Robert; Hauser, Günter; Hirsemann, Helmut; Holl, Peter; Hunter, Mark S; Kassemeyer, Stephan; Kirian, Richard A; Lomb, Lukas; Maia, Filipe R N C; Kimmel, Nils; Martin, Andrew V; Messerschmidt, Marc; Reich, Christian; Rolles, Daniel; Rudek, Benedikt; Rudenko, A.; Schlichting, Ilme; Schulz, Joachim; Seibert, M Marvin; Shoeman, Robert L; Sierra, Raymond G; Soltau, Heike; Stern, Stephan; Strüder, Lothar; Timneanu, Nicusor; Ullrich, J.; Wang, Xiaoyu; Weidenspointner, Georg; Weierstall, Uwe; Williams, Garth J; Wunderer, Cornelia B; Fromme, Petra; Spence, John C H; Stehle, Thilo; Chapman, Henry N; Betzel, Christian; Duszenko, Michael

doi:doi:10.1038/nmeth.1859

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

In vivo protein crystallization opens new routes in structural biology

MPS-Authors

/persons/resource/persons30451

Epp, S. W.
Division Prof. Dr. Joachim H. Ullrich, MPI for Nuclear Physics, Max Planck Society;

/persons/resource/persons49160

Rudek, Benedikt
Division Prof. Dr. Joachim H. Ullrich, MPI for Nuclear Physics, Max Planck Society;

/persons/resource/persons30960

Rudenko, A.
Division Prof. Dr. Joachim H. Ullrich, MPI for Nuclear Physics, Max Planck Society;

/persons/resource/persons31125

Ullrich, J.
Division Prof. Dr. Joachim H. Ullrich, MPI for Nuclear Physics, Max Planck Society;

External Resource

http://www.nature.com/nmeth/journal/vaop/ncurrent/full/nmeth.1859.html
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Koopmann, R., Cupelli, K., Redecke, L., Nass, K., DePonte, D. P., White, T. A., et al. (2012). In vivo protein crystallization opens new routes in structural biology. Nature methods, 9(3), 259-262. doi:doi:10.1038/nmeth.1859.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-441C-6

Abstract

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.