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

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

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.1
Classification:HYDROLASE
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
DOI:10.2210/pdb4hwy/pdb

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.
Date made availableDec 5 2012
PublisherRCSB-PDB

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