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In vivo protein crystallization opens new routes in structural biology

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

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

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

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

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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: http://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.