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          Institute: MPI für medizinische Forschung     Collection: Jahbruch 2014_archival     Display Documents

ID: 681492.0, MPI für medizinische Forschung / Jahbruch 2014_archival
Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X−ray laser
Translation of Title:Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X−ray laser
Authors:Redecke, Lars; Nass, Karol; DePonte, Daniel P.; White, Thomas A.; Rehders, Dirk; Barty, Anton; Stellato, Francesco; Liang, Mengning; Barends, Thomas; Boutet, Sébastien; Williams, Garth J.; Messerschmidt, Marc; Seibert, M. Marvin; Aquila, Andrew; Arnlund, David; Bajt, Saša; Barth, Torsten; Bogan, Michael J.; Caleman, Carl; Chao, Tzu−Chiao; Doak, R. Bruce; Fleckenstein, Holger; Frank, Matthias; Fromme, Raimund; Galli, Lorenzo; Grotjohann, Ingo; Hunter, Mark S.; Johansson, Linda C.; Kassemeyer, Stephan; Katona, Gergely; Kirian, Richard A.; Koopmann, Rudolf; Kupitz, Chris; Lomb, Lukas; Martin, Andrew V.; Mogk, Stefan; Neutze, Richard; Shoeman, Robert L.; Steinbrener, Jan; Timneanu, Nicusor; Wang, Dingjie; Weierstall, Uwe; Zatsepin, Nadia A.; Spence, John C. H.; Fromme, Petra; Schlichting, Ilme; Duszenko, Michael; Betzel, Christian; Chapman, Henry N.
Date of Publication (YYYY-MM-DD):2013-01-11
Title of Journal:Science
Journal Abbrev.:Science
Issue / Number:6116
Start Page:227
End Page:230
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
External Publication Status:published
Document Type:Article
Communicated by:wkaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Molecular chaperones
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Analytical Protein Biochemistry
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Coherent diffractive imaging
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