Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser.

  title={Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser.},
  author={Lars Redecke and Karol Nass and Daniel P. Deponte and Thomas A. White and Dirk Rehders and Anton Barty and Francesco Stellato and Mengning Liang and Thomas Reinier Barends and S{\'e}bastien Boutet and Garth Brokaw RoseMarie Fagan Cele Jackson Carter C. Williams and Marc Messerschmidt and M. Marvin Seibert and Andrew Aquila and David Arnlund and Sa{\vs}a Bajt and Torsten Barth and Michael J. Bogan and Carl Caleman and Tzu-Chiao Chao and R. Bruce Doak and Holger Fleckenstein and Matthias Frank and Raimund Fromme and Lorenzo Galli and Ingo Grotjohann and Mark S Hunter and Linda Johansson and Stephan Kassemeyer and Gergely Katona and Richard A. Kirian and Rudolf Koopmann and Chris Kupitz and Lukas Lomb and Andrew V. Martin and Stefan Mogk and Richard Neutze and Robert L. Shoeman and Jan Steinbrener and Nicuşor T{\^i}mneanu and Dingjie Wang and Uwe Weierstall and Nadia A. Zatsepin and John C. H. Spence and Petra Fromme and Ilme Schlichting and Michael Duszenko and Christian Betzel and Henry N. Chapman},
  volume={339 6116},
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… CONTINUE READING