Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography

18 pags, 11 figs, 5 tabs

Detalles Bibliográficos
Autores: Pandey, Suraj, Calvey, George, Katz, Andrea M., Malla, Tek Narsingh, Koua, Faisal H. M., Martín-García, José M., Poudyal, Ishwor, Yang, Jay-How, Vakili, Mohammad, Yefanov, Oleksandr, Zielinski, Kara A., Bajt, Sasa, Awel, Salah, Doerner, Katarina, Frank, Matthias, Gelisio, Luca, Jernigan, Rebecca, Kirkwood, Henry, Kloos, Marco, Koliyadu, Jayanath, Mariani, Valerio, Miller, Mitchell D., Mills, Grant, Nelson, Garrett, Olmos, Jose L., Sadri, Alireza, Sato, Tokushi, Tolstikova, Alexandra, Xu, Weijun, Ourmazd, Abbas, Spence, John C. H., Schwander, Peter, Barty, Anton, Chapman, Henry N., Fromme, Petra, Mancuso, Adrian P., Phillips, George N., Bean, Richard, Pollack, Lois, Schmidt, Marius
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/258729
Acceso en línea:http://hdl.handle.net/10261/258729
https://api.elsevier.com/content/abstract/scopus_id/85118931472
Access Level:acceso abierto
Palabra clave:European X-ray Free-Electron Laser
X-ray crystallography
Antibiotic resistance
Ceftriaxone
Drug discovery
Enzyme kinetics
Enzyme mechanisms
Irreversible inhibition
Megahertz pulse-repetition rate
Mix-and-inject serial crystallography
Protein structure determination
Serial femtosecond crystallography
Substrate diffusion in crystals
Sulbactam
β-lactamases
id ES_da05dfee5137d4784848ec85e097ea43
oai_identifier_str oai:digital.csic.es:10261/258729
network_acronym_str ES
network_name_str España
repository_id_str
dc.title.none.fl_str_mv Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
title Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
spellingShingle Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
Pandey, Suraj
European X-ray Free-Electron Laser
X-ray crystallography
Antibiotic resistance
Ceftriaxone
Drug discovery
Enzyme kinetics
Enzyme mechanisms
Irreversible inhibition
Megahertz pulse-repetition rate
Mix-and-inject serial crystallography
Protein structure determination
Serial femtosecond crystallography
Substrate diffusion in crystals
Sulbactam
β-lactamases
title_short Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
title_full Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
title_fullStr Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
title_full_unstemmed Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
title_sort Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
dc.creator.none.fl_str_mv Pandey, Suraj
Calvey, George
Katz, Andrea M.
Malla, Tek Narsingh
Koua, Faisal H. M.
Martín-García, José M.
Poudyal, Ishwor
Yang, Jay-How
Vakili, Mohammad
Yefanov, Oleksandr
Zielinski, Kara A.
Bajt, Sasa
Awel, Salah
Doerner, Katarina
Frank, Matthias
Gelisio, Luca
Jernigan, Rebecca
Kirkwood, Henry
Kloos, Marco
Koliyadu, Jayanath
Mariani, Valerio
Miller, Mitchell D.
Mills, Grant
Nelson, Garrett
Olmos, Jose L.
Sadri, Alireza
Sato, Tokushi
Tolstikova, Alexandra
Xu, Weijun
Ourmazd, Abbas
Spence, John C. H.
Schwander, Peter
Barty, Anton
Chapman, Henry N.
Fromme, Petra
Mancuso, Adrian P.
Phillips, George N.
Bean, Richard
Pollack, Lois
Schmidt, Marius
author Pandey, Suraj
author_facet Pandey, Suraj
Calvey, George
Katz, Andrea M.
Malla, Tek Narsingh
Koua, Faisal H. M.
Martín-García, José M.
Poudyal, Ishwor
Yang, Jay-How
Vakili, Mohammad
Yefanov, Oleksandr
Zielinski, Kara A.
Bajt, Sasa
Awel, Salah
Doerner, Katarina
Frank, Matthias
Gelisio, Luca
Jernigan, Rebecca
Kirkwood, Henry
Kloos, Marco
Koliyadu, Jayanath
Mariani, Valerio
Miller, Mitchell D.
Mills, Grant
Nelson, Garrett
Olmos, Jose L.
Sadri, Alireza
Sato, Tokushi
Tolstikova, Alexandra
Xu, Weijun
Ourmazd, Abbas
Spence, John C. H.
Schwander, Peter
Barty, Anton
Chapman, Henry N.
Fromme, Petra
Mancuso, Adrian P.
Phillips, George N.
Bean, Richard
Pollack, Lois
Schmidt, Marius
author_role author
author2 Calvey, George
Katz, Andrea M.
Malla, Tek Narsingh
Koua, Faisal H. M.
Martín-García, José M.
Poudyal, Ishwor
Yang, Jay-How
Vakili, Mohammad
Yefanov, Oleksandr
Zielinski, Kara A.
Bajt, Sasa
Awel, Salah
Doerner, Katarina
Frank, Matthias
Gelisio, Luca
Jernigan, Rebecca
Kirkwood, Henry
Kloos, Marco
Koliyadu, Jayanath
Mariani, Valerio
Miller, Mitchell D.
Mills, Grant
Nelson, Garrett
Olmos, Jose L.
Sadri, Alireza
Sato, Tokushi
Tolstikova, Alexandra
Xu, Weijun
Ourmazd, Abbas
Spence, John C. H.
Schwander, Peter
Barty, Anton
Chapman, Henry N.
Fromme, Petra
Mancuso, Adrian P.
Phillips, George N.
Bean, Richard
Pollack, Lois
Schmidt, Marius
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
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author
dc.contributor.none.fl_str_mv National Science Foundation (US)
Department of Energy (US)
National Institutes of Health (US)
Lawrence Livermore National Laboratory
German Research Foundation
European Commission
European Research Council
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv European X-ray Free-Electron Laser
X-ray crystallography
Antibiotic resistance
Ceftriaxone
Drug discovery
Enzyme kinetics
Enzyme mechanisms
Irreversible inhibition

Megahertz pulse-repetition rate
Mix-and-inject serial crystallography
Protein structure determination
Serial femtosecond crystallography
Substrate diffusion in crystals
Sulbactam
β-lactamases
topic European X-ray Free-Electron Laser
X-ray crystallography
Antibiotic resistance
Ceftriaxone
Drug discovery
Enzyme kinetics
Enzyme mechanisms
Irreversible inhibition
Megahertz pulse-repetition rate
Mix-and-inject serial crystallography
Protein structure determination
Serial femtosecond crystallography
Substrate diffusion in crystals
Sulbactam
β-lactamases
description 18 pags, 11 figs, 5 tabs
publishDate 2021
dc.date.none.fl_str_mv 2021
2022
2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/258729
https://api.elsevier.com/content/abstract/scopus_id/85118931472
url http://hdl.handle.net/10261/258729
https://api.elsevier.com/content/abstract/scopus_id/85118931472
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/EC/H2020/637295
info:eu-repo/grantAgreement/EC/FP7/609920
IUCrJ
https://doi.org/10.1107/S2052252521008125

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv International Union of Crystallography
publisher.none.fl_str_mv International Union of Crystallography
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869421490656509952
spelling Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallographyPandey, SurajCalvey, GeorgeKatz, Andrea M.Malla, Tek NarsinghKoua, Faisal H. M.Martín-García, José M.Poudyal, IshworYang, Jay-HowVakili, MohammadYefanov, OleksandrZielinski, Kara A.Bajt, SasaAwel, SalahDoerner, KatarinaFrank, MatthiasGelisio, LucaJernigan, RebeccaKirkwood, HenryKloos, MarcoKoliyadu, JayanathMariani, ValerioMiller, Mitchell D.Mills, GrantNelson, GarrettOlmos, Jose L.Sadri, AlirezaSato, TokushiTolstikova, AlexandraXu, WeijunOurmazd, AbbasSpence, John C. H.Schwander, PeterBarty, AntonChapman, Henry N.Fromme, PetraMancuso, Adrian P.Phillips, George N.Bean, RichardPollack, LoisSchmidt, MariusEuropean X-ray Free-Electron LaserX-ray crystallographyAntibiotic resistanceCeftriaxoneDrug discoveryEnzyme kineticsEnzyme mechanismsIrreversible inhibitionMegahertz pulse-repetition rateMix-and-inject serial crystallographyProtein structure determinationSerial femtosecond crystallographySubstrate diffusion in crystalsSulbactamβ-lactamases18 pags, 11 figs, 5 tabsHere, we illustrate what happens inside the catalytic cleft of an enzyme when substrate or ligand binds on single-millisecond timescales. The initial phase of the enzymatic cycle is observed with near-atomic resolution using the most advanced X-ray source currently available: the European XFEL (EuXFEL). The high repetition rate of the EuXFEL combined with our mix-and-inject technology enables the initial phase of ceftriaxone binding to the Mycobacterium tuberculosis β-lactamase to be followed using time-resolved crystallography in real time. It is shown how a diffusion coefficient in enzyme crystals can be derived directly from the X-ray data, enabling the determination of ligand and enzyme-ligand concentrations at any position in the crystal volume as a function of time. In addition, the structure of the irreversible inhibitor sulbactam bound to the enzyme at a 66 ms time delay after mixing is described. This demonstrates that the EuXFEL can be used as an important tool for biomedically relevant research.This work was supported by the National Science Foundation Science and Technology Center 'BioXFEL' through award STC-1231306, and in part by the US Department of Energy, Office of Science, Basic Energy Sciences under contract DESC0002164 (AO, algorithm design and development) and by the National Science Foundation under contract Nos. 1551489 (AO, underlying analytical models) and DBI-2029533 (AO, functional conformations). This material is based upon work supported by the National Science Foundation Graduate Research Fellowship Program under Grant No. 1450681 to JLO. The work was also supported by funds from the National Institutes of Health grant R01 GM117342-0404. Funding and support are also acknowledged from the National Institutes of Health grant R01 GM095583, from the Biodesign Center for Applied Structural Discovery at ASU, from National Science Foundation award No. 1565180 and the US Department of Energy through Lawrence Livermore National Laboratory under contract DE-AC52-07NA27344. KAZ was supported by the Cornell Molecular Biophysics Training Program (NIH T32-GM008267). This work was also supported by the Cluster of Excellence 'CUI: Advanced Imaging of Matter' of the Deutsche Forschungsgemeinschaft (DFG), EXC 2056, project ID 390715994. CFEL is supported by the Gottfried Wilhelm Leibniz Program of the DFG, the 'X-probe' project funded by the European Union 2020 Research and Innovation Program under Marie Sklodowska-Curie grant agreement 637295, the European Research Council, 'Frontiers in Attosecond X-ray Science: Imaging and Spectroscopy (AXSIS)', ERC-2013-SyG 609920, and the Human Frontiers Science Program grant RGP0010 2017. This work is also supported by the AXSIS project funded by the European Research Council under the European Union Seventh Framework Program (FP/2007-2013)/ERC Grant Agreement No. 609920.Peer reviewedInternational Union of CrystallographyNational Science Foundation (US)Department of Energy (US)National Institutes of Health (US)Lawrence Livermore National LaboratoryGerman Research FoundationEuropean CommissionEuropean Research CouncilConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202220222021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/258729https://api.elsevier.com/content/abstract/scopus_id/85118931472reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/EC/H2020/637295info:eu-repo/grantAgreement/EC/FP7/609920IUCrJhttps://doi.org/10.1107/S2052252521008125Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2587292026-05-22T06:33:51Z
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