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Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser

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

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Barends,  Thomas R.M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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

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

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

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

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Steinbrener,  Jan
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;

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Citation

Redecke, L., Nass, K., DePonte, D. P., White, T. A., Rehders, D., Barty, A., et al. (2013). Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser. Science, 339(6116), 227-230. doi:10.1126/science.1229663.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-085B-1
Abstract
The Trypanosoma brucei cysteine protease cathepsin B (TbCatB), which is involved in host protein degradation, is a promising target to develop new treatments against sleeping sickness, a fatal disease caused by this protozoan parasite. The structure of the mature, active form of TbCatB has so far not provided sufficient information for the design of a safe and specific drug against T. brucei. By combining two recent innovations, in vivo crystallization and serial femtosecond crystallography, we obtained the room−temperature 2.1 angstrom resolution structure of the fully glycosylated precursor complex of TbCatB. The structure reveals the mechanism of native TbCatB inhibition and demonstrates that new biomolecular information can be obtained by the "diffraction−before−destruction" approach of x−ray free−electron lasers from hundreds of thousands of individual microcrystals