Natively inhibited trypanosoma brucei cathepsin B structure determined by using an x-ray laser

Redecke, L, Nass, K, DePonte, D, White, T and Martin, A 2013, 'Natively inhibited trypanosoma brucei cathepsin B structure determined by using an x-ray laser', Science, vol. 339, no. 6116, pp. 227-230.


Document type: Journal Article
Collection: Journal Articles

Title Natively inhibited trypanosoma brucei cathepsin B structure determined by using an x-ray laser
Author(s) Redecke, L
Nass, K
DePonte, D
White, T
Martin, A
Year 2013
Journal name Science
Volume number 339
Issue number 6116
Start page 227
End page 230
Total pages 4
Publisher American Association for the Advancement of Science (A A A S)
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.
Subject Condensed Matter Imaging
DOI - identifier 10.1126/science.1229663
Copyright notice ©
ISSN 0036-8075
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