Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography
Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Jose L. Olmos [verfasserIn] Suraj Pandey [verfasserIn] Jose M. Martin-Garcia [verfasserIn] George Calvey [verfasserIn] Andrea Katz [verfasserIn] Juraj Knoska [verfasserIn] Christopher Kupitz [verfasserIn] Mark S. Hunter [verfasserIn] Mengning Liang [verfasserIn] Dominik Oberthuer [verfasserIn] Oleksandr Yefanov [verfasserIn] Max Wiedorn [verfasserIn] Michael Heyman [verfasserIn] Mark Holl [verfasserIn] Kanupriya Pande [verfasserIn] Anton Barty [verfasserIn] Mitchell D. Miller [verfasserIn] Stephan Stern [verfasserIn] Shatabdi Roy-Chowdhury [verfasserIn] Jesse Coe [verfasserIn] Nirupa Nagaratnam [verfasserIn] James Zook [verfasserIn] Jacob Verburgt [verfasserIn] Tyler Norwood [verfasserIn] Ishwor Poudyal [verfasserIn] David Xu [verfasserIn] Jason Koglin [verfasserIn] Matthew H. Seaberg [verfasserIn] Yun Zhao [verfasserIn] Saša Bajt [verfasserIn] Thomas Grant [verfasserIn] Valerio Mariani [verfasserIn] Garrett Nelson [verfasserIn] Ganesh Subramanian [verfasserIn] Euiyoung Bae [verfasserIn] Raimund Fromme [verfasserIn] Russell Fung [verfasserIn] Peter Schwander [verfasserIn] Matthias Frank [verfasserIn] Thomas A. White [verfasserIn] Uwe Weierstall [verfasserIn] Nadia Zatsepin [verfasserIn] John Spence [verfasserIn] Petra Fromme [verfasserIn] Henry N. Chapman [verfasserIn] Lois Pollack [verfasserIn] Lee Tremblay [verfasserIn] Abbas Ourmazd [verfasserIn] George N. Phillips [verfasserIn] Marius Schmidt [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2018 |
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| Übergeordnetes Werk: |
In: BMC Biology - BMC, 2003, 16(2018), 1, Seite 15 |
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| Übergeordnetes Werk: |
volume:16 ; year:2018 ; number:1 ; pages:15 |
| Links: |
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| DOI / URN: |
10.1186/s12915-018-0524-5 |
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| Katalog-ID: |
DOAJ070827621 |
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| 245 | 1 | 0 | |a Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography |
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| 520 | |a Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. | ||
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10.1186/s12915-018-0524-5 doi (DE-627)DOAJ070827621 (DE-599)DOAJcc4fc7b9369349448afd757a6952a22b DE-627 ger DE-627 rakwb eng QH301-705.5 Jose L. Olmos verfasserin aut Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. Biology (General) Suraj Pandey verfasserin aut Jose M. Martin-Garcia verfasserin aut George Calvey verfasserin aut Andrea Katz verfasserin aut Juraj Knoska verfasserin aut Christopher Kupitz verfasserin aut Mark S. Hunter verfasserin aut Mengning Liang verfasserin aut Dominik Oberthuer verfasserin aut Oleksandr Yefanov verfasserin aut Max Wiedorn verfasserin aut Michael Heyman verfasserin aut Mark Holl verfasserin aut Kanupriya Pande verfasserin aut Anton Barty verfasserin aut Mitchell D. Miller verfasserin aut Stephan Stern verfasserin aut Shatabdi Roy-Chowdhury verfasserin aut Jesse Coe verfasserin aut Nirupa Nagaratnam verfasserin aut James Zook verfasserin aut Jacob Verburgt verfasserin aut Tyler Norwood verfasserin aut Ishwor Poudyal verfasserin aut David Xu verfasserin aut Jason Koglin verfasserin aut Matthew H. Seaberg verfasserin aut Yun Zhao verfasserin aut Saša Bajt verfasserin aut Thomas Grant verfasserin aut Valerio Mariani verfasserin aut Garrett Nelson verfasserin aut Ganesh Subramanian verfasserin aut Euiyoung Bae verfasserin aut Raimund Fromme verfasserin aut Russell Fung verfasserin aut Peter Schwander verfasserin aut Matthias Frank verfasserin aut Thomas A. White verfasserin aut Uwe Weierstall verfasserin aut Nadia Zatsepin verfasserin aut John Spence verfasserin aut Petra Fromme verfasserin aut Henry N. Chapman verfasserin aut Lois Pollack verfasserin aut Lee Tremblay verfasserin aut Abbas Ourmazd verfasserin aut George N. Phillips verfasserin aut Marius Schmidt verfasserin aut In BMC Biology BMC, 2003 16(2018), 1, Seite 15 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:16 year:2018 number:1 pages:15 https://doi.org/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/article/cc4fc7b9369349448afd757a6952a22b kostenfrei http://link.springer.com/article/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 16 2018 1 15 |
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10.1186/s12915-018-0524-5 doi (DE-627)DOAJ070827621 (DE-599)DOAJcc4fc7b9369349448afd757a6952a22b DE-627 ger DE-627 rakwb eng QH301-705.5 Jose L. Olmos verfasserin aut Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. Biology (General) Suraj Pandey verfasserin aut Jose M. Martin-Garcia verfasserin aut George Calvey verfasserin aut Andrea Katz verfasserin aut Juraj Knoska verfasserin aut Christopher Kupitz verfasserin aut Mark S. Hunter verfasserin aut Mengning Liang verfasserin aut Dominik Oberthuer verfasserin aut Oleksandr Yefanov verfasserin aut Max Wiedorn verfasserin aut Michael Heyman verfasserin aut Mark Holl verfasserin aut Kanupriya Pande verfasserin aut Anton Barty verfasserin aut Mitchell D. Miller verfasserin aut Stephan Stern verfasserin aut Shatabdi Roy-Chowdhury verfasserin aut Jesse Coe verfasserin aut Nirupa Nagaratnam verfasserin aut James Zook verfasserin aut Jacob Verburgt verfasserin aut Tyler Norwood verfasserin aut Ishwor Poudyal verfasserin aut David Xu verfasserin aut Jason Koglin verfasserin aut Matthew H. Seaberg verfasserin aut Yun Zhao verfasserin aut Saša Bajt verfasserin aut Thomas Grant verfasserin aut Valerio Mariani verfasserin aut Garrett Nelson verfasserin aut Ganesh Subramanian verfasserin aut Euiyoung Bae verfasserin aut Raimund Fromme verfasserin aut Russell Fung verfasserin aut Peter Schwander verfasserin aut Matthias Frank verfasserin aut Thomas A. White verfasserin aut Uwe Weierstall verfasserin aut Nadia Zatsepin verfasserin aut John Spence verfasserin aut Petra Fromme verfasserin aut Henry N. Chapman verfasserin aut Lois Pollack verfasserin aut Lee Tremblay verfasserin aut Abbas Ourmazd verfasserin aut George N. Phillips verfasserin aut Marius Schmidt verfasserin aut In BMC Biology BMC, 2003 16(2018), 1, Seite 15 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:16 year:2018 number:1 pages:15 https://doi.org/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/article/cc4fc7b9369349448afd757a6952a22b kostenfrei http://link.springer.com/article/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 16 2018 1 15 |
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10.1186/s12915-018-0524-5 doi (DE-627)DOAJ070827621 (DE-599)DOAJcc4fc7b9369349448afd757a6952a22b DE-627 ger DE-627 rakwb eng QH301-705.5 Jose L. Olmos verfasserin aut Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. Biology (General) Suraj Pandey verfasserin aut Jose M. Martin-Garcia verfasserin aut George Calvey verfasserin aut Andrea Katz verfasserin aut Juraj Knoska verfasserin aut Christopher Kupitz verfasserin aut Mark S. Hunter verfasserin aut Mengning Liang verfasserin aut Dominik Oberthuer verfasserin aut Oleksandr Yefanov verfasserin aut Max Wiedorn verfasserin aut Michael Heyman verfasserin aut Mark Holl verfasserin aut Kanupriya Pande verfasserin aut Anton Barty verfasserin aut Mitchell D. Miller verfasserin aut Stephan Stern verfasserin aut Shatabdi Roy-Chowdhury verfasserin aut Jesse Coe verfasserin aut Nirupa Nagaratnam verfasserin aut James Zook verfasserin aut Jacob Verburgt verfasserin aut Tyler Norwood verfasserin aut Ishwor Poudyal verfasserin aut David Xu verfasserin aut Jason Koglin verfasserin aut Matthew H. Seaberg verfasserin aut Yun Zhao verfasserin aut Saša Bajt verfasserin aut Thomas Grant verfasserin aut Valerio Mariani verfasserin aut Garrett Nelson verfasserin aut Ganesh Subramanian verfasserin aut Euiyoung Bae verfasserin aut Raimund Fromme verfasserin aut Russell Fung verfasserin aut Peter Schwander verfasserin aut Matthias Frank verfasserin aut Thomas A. White verfasserin aut Uwe Weierstall verfasserin aut Nadia Zatsepin verfasserin aut John Spence verfasserin aut Petra Fromme verfasserin aut Henry N. Chapman verfasserin aut Lois Pollack verfasserin aut Lee Tremblay verfasserin aut Abbas Ourmazd verfasserin aut George N. Phillips verfasserin aut Marius Schmidt verfasserin aut In BMC Biology BMC, 2003 16(2018), 1, Seite 15 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:16 year:2018 number:1 pages:15 https://doi.org/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/article/cc4fc7b9369349448afd757a6952a22b kostenfrei http://link.springer.com/article/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 16 2018 1 15 |
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10.1186/s12915-018-0524-5 doi (DE-627)DOAJ070827621 (DE-599)DOAJcc4fc7b9369349448afd757a6952a22b DE-627 ger DE-627 rakwb eng QH301-705.5 Jose L. Olmos verfasserin aut Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. Biology (General) Suraj Pandey verfasserin aut Jose M. Martin-Garcia verfasserin aut George Calvey verfasserin aut Andrea Katz verfasserin aut Juraj Knoska verfasserin aut Christopher Kupitz verfasserin aut Mark S. Hunter verfasserin aut Mengning Liang verfasserin aut Dominik Oberthuer verfasserin aut Oleksandr Yefanov verfasserin aut Max Wiedorn verfasserin aut Michael Heyman verfasserin aut Mark Holl verfasserin aut Kanupriya Pande verfasserin aut Anton Barty verfasserin aut Mitchell D. Miller verfasserin aut Stephan Stern verfasserin aut Shatabdi Roy-Chowdhury verfasserin aut Jesse Coe verfasserin aut Nirupa Nagaratnam verfasserin aut James Zook verfasserin aut Jacob Verburgt verfasserin aut Tyler Norwood verfasserin aut Ishwor Poudyal verfasserin aut David Xu verfasserin aut Jason Koglin verfasserin aut Matthew H. Seaberg verfasserin aut Yun Zhao verfasserin aut Saša Bajt verfasserin aut Thomas Grant verfasserin aut Valerio Mariani verfasserin aut Garrett Nelson verfasserin aut Ganesh Subramanian verfasserin aut Euiyoung Bae verfasserin aut Raimund Fromme verfasserin aut Russell Fung verfasserin aut Peter Schwander verfasserin aut Matthias Frank verfasserin aut Thomas A. White verfasserin aut Uwe Weierstall verfasserin aut Nadia Zatsepin verfasserin aut John Spence verfasserin aut Petra Fromme verfasserin aut Henry N. Chapman verfasserin aut Lois Pollack verfasserin aut Lee Tremblay verfasserin aut Abbas Ourmazd verfasserin aut George N. Phillips verfasserin aut Marius Schmidt verfasserin aut In BMC Biology BMC, 2003 16(2018), 1, Seite 15 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:16 year:2018 number:1 pages:15 https://doi.org/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/article/cc4fc7b9369349448afd757a6952a22b kostenfrei http://link.springer.com/article/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 16 2018 1 15 |
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10.1186/s12915-018-0524-5 doi (DE-627)DOAJ070827621 (DE-599)DOAJcc4fc7b9369349448afd757a6952a22b DE-627 ger DE-627 rakwb eng QH301-705.5 Jose L. Olmos verfasserin aut Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. Biology (General) Suraj Pandey verfasserin aut Jose M. Martin-Garcia verfasserin aut George Calvey verfasserin aut Andrea Katz verfasserin aut Juraj Knoska verfasserin aut Christopher Kupitz verfasserin aut Mark S. Hunter verfasserin aut Mengning Liang verfasserin aut Dominik Oberthuer verfasserin aut Oleksandr Yefanov verfasserin aut Max Wiedorn verfasserin aut Michael Heyman verfasserin aut Mark Holl verfasserin aut Kanupriya Pande verfasserin aut Anton Barty verfasserin aut Mitchell D. Miller verfasserin aut Stephan Stern verfasserin aut Shatabdi Roy-Chowdhury verfasserin aut Jesse Coe verfasserin aut Nirupa Nagaratnam verfasserin aut James Zook verfasserin aut Jacob Verburgt verfasserin aut Tyler Norwood verfasserin aut Ishwor Poudyal verfasserin aut David Xu verfasserin aut Jason Koglin verfasserin aut Matthew H. Seaberg verfasserin aut Yun Zhao verfasserin aut Saša Bajt verfasserin aut Thomas Grant verfasserin aut Valerio Mariani verfasserin aut Garrett Nelson verfasserin aut Ganesh Subramanian verfasserin aut Euiyoung Bae verfasserin aut Raimund Fromme verfasserin aut Russell Fung verfasserin aut Peter Schwander verfasserin aut Matthias Frank verfasserin aut Thomas A. White verfasserin aut Uwe Weierstall verfasserin aut Nadia Zatsepin verfasserin aut John Spence verfasserin aut Petra Fromme verfasserin aut Henry N. Chapman verfasserin aut Lois Pollack verfasserin aut Lee Tremblay verfasserin aut Abbas Ourmazd verfasserin aut George N. Phillips verfasserin aut Marius Schmidt verfasserin aut In BMC Biology BMC, 2003 16(2018), 1, Seite 15 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:16 year:2018 number:1 pages:15 https://doi.org/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/article/cc4fc7b9369349448afd757a6952a22b kostenfrei http://link.springer.com/article/10.1186/s12915-018-0524-5 kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 16 2018 1 15 |
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Jose L. Olmos @@aut@@ Suraj Pandey @@aut@@ Jose M. Martin-Garcia @@aut@@ George Calvey @@aut@@ Andrea Katz @@aut@@ Juraj Knoska @@aut@@ Christopher Kupitz @@aut@@ Mark S. Hunter @@aut@@ Mengning Liang @@aut@@ Dominik Oberthuer @@aut@@ Oleksandr Yefanov @@aut@@ Max Wiedorn @@aut@@ Michael Heyman @@aut@@ Mark Holl @@aut@@ Kanupriya Pande @@aut@@ Anton Barty @@aut@@ Mitchell D. Miller @@aut@@ Stephan Stern @@aut@@ Shatabdi Roy-Chowdhury @@aut@@ Jesse Coe @@aut@@ Nirupa Nagaratnam @@aut@@ James Zook @@aut@@ Jacob Verburgt @@aut@@ Tyler Norwood @@aut@@ Ishwor Poudyal @@aut@@ David Xu @@aut@@ Jason Koglin @@aut@@ Matthew H. Seaberg @@aut@@ Yun Zhao @@aut@@ Saša Bajt @@aut@@ Thomas Grant @@aut@@ Valerio Mariani @@aut@@ Garrett Nelson @@aut@@ Ganesh Subramanian @@aut@@ Euiyoung Bae @@aut@@ Raimund Fromme @@aut@@ Russell Fung @@aut@@ Peter Schwander @@aut@@ Matthias Frank @@aut@@ Thomas A. White @@aut@@ Uwe Weierstall @@aut@@ Nadia Zatsepin @@aut@@ John Spence @@aut@@ Petra Fromme @@aut@@ Henry N. Chapman @@aut@@ Lois Pollack @@aut@@ Lee Tremblay @@aut@@ Abbas Ourmazd @@aut@@ George N. Phillips @@aut@@ Marius Schmidt @@aut@@ |
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Olmos</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2018</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. 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Jose L. Olmos |
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Jose L. Olmos misc QH301-705.5 misc Biology (General) Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography |
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QH301-705.5 Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography |
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Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography |
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Jose L. Olmos Suraj Pandey Jose M. Martin-Garcia George Calvey Andrea Katz Juraj Knoska Christopher Kupitz Mark S. Hunter Mengning Liang Dominik Oberthuer Oleksandr Yefanov Max Wiedorn Michael Heyman Mark Holl Kanupriya Pande Anton Barty Mitchell D. Miller Stephan Stern Shatabdi Roy-Chowdhury Jesse Coe Nirupa Nagaratnam James Zook Jacob Verburgt Tyler Norwood Ishwor Poudyal David Xu Jason Koglin Matthew H. Seaberg Yun Zhao Saša Bajt Thomas Grant Valerio Mariani Garrett Nelson Ganesh Subramanian Euiyoung Bae Raimund Fromme Russell Fung Peter Schwander Matthias Frank Thomas A. White Uwe Weierstall Nadia Zatsepin John Spence Petra Fromme Henry N. Chapman Lois Pollack Lee Tremblay Abbas Ourmazd George N. Phillips Marius Schmidt |
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10.1186/s12915-018-0524-5 |
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enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography |
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QH301-705.5 |
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Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography |
| abstract |
Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. |
| abstractGer |
Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. |
| abstract_unstemmed |
Abstract Background Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. Results Here, we demonstrate a general method for capturing enzyme catalysis “in action” by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. Conclusions MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data. |
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Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography |
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https://doi.org/10.1186/s12915-018-0524-5 https://doaj.org/article/cc4fc7b9369349448afd757a6952a22b http://link.springer.com/article/10.1186/s12915-018-0524-5 https://doaj.org/toc/1741-7007 |
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Suraj Pandey Jose M. Martin-Garcia George Calvey Andrea Katz Juraj Knoska Christopher Kupitz Mark S. Hunter Mengning Liang Dominik Oberthuer Oleksandr Yefanov Max Wiedorn Michael Heyman Mark Holl Kanupriya Pande Anton Barty Mitchell D. Miller Stephan Stern Shatabdi Roy-Chowdhury Jesse Coe Nirupa Nagaratnam James Zook Jacob Verburgt Tyler Norwood Ishwor Poudyal David Xu Jason Koglin Matthew H. Seaberg Yun Zhao Saša Bajt Thomas Grant Valerio Mariani Garrett Nelson Ganesh Subramanian Euiyoung Bae Raimund Fromme Russell Fung Peter Schwander Matthias Frank Thomas A. White Uwe Weierstall Nadia Zatsepin John Spence Petra Fromme Henry N. Chapman Lois Pollack Lee Tremblay Abbas Ourmazd George N. Phillips Marius Schmidt |
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Suraj Pandey Jose M. Martin-Garcia George Calvey Andrea Katz Juraj Knoska Christopher Kupitz Mark S. Hunter Mengning Liang Dominik Oberthuer Oleksandr Yefanov Max Wiedorn Michael Heyman Mark Holl Kanupriya Pande Anton Barty Mitchell D. Miller Stephan Stern Shatabdi Roy-Chowdhury Jesse Coe Nirupa Nagaratnam James Zook Jacob Verburgt Tyler Norwood Ishwor Poudyal David Xu Jason Koglin Matthew H. Seaberg Yun Zhao Saša Bajt Thomas Grant Valerio Mariani Garrett Nelson Ganesh Subramanian Euiyoung Bae Raimund Fromme Russell Fung Peter Schwander Matthias Frank Thomas A. White Uwe Weierstall Nadia Zatsepin John Spence Petra Fromme Henry N. Chapman Lois Pollack Lee Tremblay Abbas Ourmazd George N. Phillips Marius Schmidt |
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10.1186/s12915-018-0524-5 |
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2024-07-03T16:55:49.589Z |
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| score |
7.399766 |