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

Redecke, L., Nass, K., DePonte, D. P., White, T. A., Rehders, D., Barty, A., et al. (2013). Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser. Science, 339(6116), 227-230. doi:10.1126/science.1229663.

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Genre: Journal Article
Alternative Title : Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser

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Redecke, Lars, Author
Nass, Karol1, Author              
DePonte, Daniel P., Author
White, Thomas A., Author
Rehders, Dirk, Author
Barty, Anton, Author
Stellato, Francesco, Author
Liang, Mengning, Author
Barends, Thomas R.M.1, Author              
Boutet, Sébastien, Author
Williams, Garth J., Author
Messerschmidt, Marc, Author
Seibert, M. Marvin, Author
Aquila, Andrew, Author
Arnlund, David, Author
Bajt, Saša, Author
Barth, Torsten, Author
Bogan, Michael J., Author
Caleman, Carl, Author
Chao, Tzu−Chiao, Author
Doak, R. Bruce1, Author              Fleckenstein, Holger, AuthorFrank, Matthias, AuthorFromme, Raimund, AuthorGalli, Lorenzo, AuthorGrotjohann, Ingo, AuthorHunter, Mark S., AuthorJohansson, Linda C., AuthorKassemeyer, Stephan1, Author              Katona, Gergely, AuthorKirian, Richard A., AuthorKoopmann, Rudolf, AuthorKupitz, Chris, AuthorLomb, Lukas1, Author              Martin, Andrew V., AuthorMogk, Stefan, AuthorNeutze, Richard, AuthorShoeman, Robert L.1, Author              Steinbrener, Jan1, Author              Timneanu, Nicusor, AuthorWang, Dingjie, AuthorWeierstall, Uwe, AuthorZatsepin, Nadia A., AuthorSpence, John C. H., AuthorFromme, Petra, AuthorSchlichting, Ilme1, Author              Duszenko, Michael, AuthorBetzel, Christian, AuthorChapman, Henry N., Author more..
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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

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Language(s): eng - English
 Dates: 2012-09-032012-11-142012-11-292013-01-11
 Publication Status: Published in print
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 Rev. Type: Peer
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Title: Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 339 (6116) Sequence Number: - Start / End Page: 227 - 230 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1