{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Redecke L"],"funding":["Office of Basic Energy Sciences","National Institutes of Health","NIGMS NIH HHS","National Science Foundation","U.S. Department of Education"],"pagination":["227-230"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3786669"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["339(6116)"],"pubmed_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 o"],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser."],"pmcid":["PMC3786669"],"funding_grant_id":["1R01GM095583","MCB-1021557","MCB-1120997","U54 GM094599","R01 GM095583","DE-AC52-07NA27344"],"pubmed_authors":["Martin AV","Doak RB","Caleman C","Barty A","Wang D","Betzel C","Williams GJ","DePonte DP","Shoeman RL","Frank M","Liang M","Timneanu N","Chapman HN","Stellato F","Schlichting I","Galli L","Grotjohann I","Fromme R","Messerschmidt M","Fromme P","White TA","Kassemeyer S","Zatsepin NA","Steinbrener J","Bogan MJ","Koopmann R","Spence JCH","Barth T","Kirian RA","Barends TRM","Weierstall U","Duszenko M","Aquila A","Lomb L","Neutze R","Kupitz C","Arnlund D","Redecke L","Seibert MM","Fleckenstein H","Rehders D","Mogk S","Johansson LC","Hunter MS","Boutet S","Bajt S","Nass K","Katona G","Chao TC"],"additional_accession":[]},"is_claimable":false,"name":"Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser.","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 o","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Jan","modification":"2026-05-03T22:24:58.208Z","creation":"2019-03-27T01:16:42Z"},"accession":"S-EPMC3786669","cross_references":{"pubmed":["23196907"],"doi":["10.1126/science.1229663"]}}