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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
