Journal
SCIENCE
Volume 339, Issue 6116, Pages 227-230Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1229663
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Funding
- German Federal Ministry for Education and Research [01KX0806, 01KX0807]
- Hamburg Ministry of Science and Research
- Joachim Herz Stiftung, Hamburg Initiative for Excellence in Research
- Hamburg School for Structure and Dynamics in Infection (SDI)
- Deutsche Forschungsgemeinschaft (DFG) Cluster of Excellence Inflammation at interfaces [EXC 306]
- DFG
- Landesgraduiertenforderung Baden-Wurttemberg
- Max Planck Society
- Swedish Research Council
- Swedish Strategic Research Foundation
- Swedish Foundation for International Cooperation in Research and Higher Education
- U.S. Department of Energy Office of Basic Energy Sciences through PULSE Institute at SLAC
- U.S. Department of Energy through Lawrence Livermore National Laboratory [DE-AC52-07NA27344]
- University of California Office of the President Lab Fee Program [118036]
- NSF [MCB-1021557, MCB-1120997]
- NIH [1R01GM095583]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1021557, 1120997] Funding Source: National Science Foundation
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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.
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