4HWY : Trypanosoma brucei procathepsin B solved from 40 fs free-electron laser pulse data by serial femtosecond X-ray crystallography

  • Lars Redecke (Contributor)
  • Karol Nass (Contributor)
  • D. P. Deponte (Contributor)
  • Thomas A. White (Contributor)
  • Dirk Rehders (Contributor)
  • Anton Barty (Contributor)
  • Francesco Stellato (Contributor)
  • Mengning Liang (Contributor)
  • Thomas R M Barends (Contributor)
  • S├ębastien Boutet (Contributor)
  • Garth J. Williams (Contributor)
  • Marc Messerschmidt (Contributor)
  • M. Marvin Seibert (Contributor)
  • Andrew Aquila (Contributor)
  • David Arnlund (Contributor)
  • Sasa Bajt (Contributor)
  • Torsten B. Barth (Contributor)
  • Michael J. Bogan (Contributor)
  • Carl Caleman (Contributor)
  • T. C. Chao (Contributor)
  • R. B. Doak (Contributor)
  • Holger Fleckenstein (Contributor)
  • Matthias Frank (Contributor)
  • Raimund Fromme (Contributor)
  • Lorenzo Galli (Contributor)
  • Ingo Grotjohann (Contributor)
  • Mark S. Hunter (Contributor)
  • Linda C. Johansson (Contributor)
  • Stephan Kassemeyer (Contributor)
  • Gergely Katona (Contributor)
  • Richard Kirian (Contributor)
  • Rudolf Koopmann (Contributor)
  • Christopher Kupitz (Contributor)
  • Lukas Lomb (Contributor)
  • Andrew V. Martin (Contributor)
  • Stefan Mogk (Contributor)
  • Richard Neutze (Contributor)
  • Robert L. Shoeman (Contributor)
  • Jan Steinbrener (Contributor)
  • Nicusor Timneanu (Contributor)
  • Dingjie Wang (Contributor)
  • Uwe Weierstall (Contributor)
  • Nadia A. Zatsepin (Contributor)
  • John C. H. Spence (Contributor)
  • Petra Fromme (Contributor)
  • Ilme Schlichting (Contributor)
  • Michael Duszenko (Contributor)
  • Christian Betzel (Contributor)
  • Henry N. Chapman (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2012-12-05
Deposition Date:2012-11-09
Revision Date:2012-12-19#2013-01-23#2016-12-21#2017-11-15#2018-02-14
Molecular Weight:38324.68
Macromolecule Type:Protein
Residue Count:340
Atom Site Count:2453

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.
Date made available2012

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