An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography
Currently many of the time resolved serial femtosecond (SFX) crystallography experiments are done with light driven protein systems, whereas the reaction initiation for non-light triggered enzymes remains a major bottle neck. Here, the authors present an expanded Drop-on-Tape system, where picoliter...
| Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-24757-7 |
| _version_ | 1828955468260704256 |
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| author | Agata Butryn Philipp S. Simon Pierre Aller Philip Hinchliffe Ramzi N. Massad Gabriel Leen Catherine L. Tooke Isabel Bogacz In-Sik Kim Asmit Bhowmick Aaron S. Brewster Nicholas E. Devenish Jürgen Brem Jos J. A. G. Kamps Pauline A. Lang Patrick Rabe Danny Axford John H. Beale Bradley Davy Ali Ebrahim Julien Orlans Selina L. S. Storm Tiankun Zhou Shigeki Owada Rie Tanaka Kensuke Tono Gwyndaf Evans Robin L. Owen Frances A. Houle Nicholas K. Sauter Christopher J. Schofield James Spencer Vittal K. Yachandra Junko Yano Jan F. Kern Allen M. Orville |
| author_facet | Agata Butryn Philipp S. Simon Pierre Aller Philip Hinchliffe Ramzi N. Massad Gabriel Leen Catherine L. Tooke Isabel Bogacz In-Sik Kim Asmit Bhowmick Aaron S. Brewster Nicholas E. Devenish Jürgen Brem Jos J. A. G. Kamps Pauline A. Lang Patrick Rabe Danny Axford John H. Beale Bradley Davy Ali Ebrahim Julien Orlans Selina L. S. Storm Tiankun Zhou Shigeki Owada Rie Tanaka Kensuke Tono Gwyndaf Evans Robin L. Owen Frances A. Houle Nicholas K. Sauter Christopher J. Schofield James Spencer Vittal K. Yachandra Junko Yano Jan F. Kern Allen M. Orville |
| author_sort | Agata Butryn |
| collection | DOAJ |
| description | Currently many of the time resolved serial femtosecond (SFX) crystallography experiments are done with light driven protein systems, whereas the reaction initiation for non-light triggered enzymes remains a major bottle neck. Here, the authors present an expanded Drop-on-Tape system, where picoliter-sized droplets of a substrate or inhibitor are turbulently mixed with nanoliter sized droplets of microcrystal slurries, and they use it for time-resolved SFX measurements of inhibitor binding to lysozyme and secondly, binding of a β-lactam antibiotic to a bacterial serine β-lactamase. |
| first_indexed | 2024-12-14T07:51:54Z |
| format | Article |
| id | doaj.art-55ce2079723b464484f4eed86828b06d |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T07:51:54Z |
| publishDate | 2021-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-55ce2079723b464484f4eed86828b06d2022-12-21T23:10:41ZengNature PortfolioNature Communications2041-17232021-07-011211710.1038/s41467-021-24757-7An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallographyAgata Butryn0Philipp S. Simon1Pierre Aller2Philip Hinchliffe3Ramzi N. Massad4Gabriel Leen5Catherine L. Tooke6Isabel Bogacz7In-Sik Kim8Asmit Bhowmick9Aaron S. Brewster10Nicholas E. Devenish11Jürgen Brem12Jos J. A. G. Kamps13Pauline A. Lang14Patrick Rabe15Danny Axford16John H. Beale17Bradley Davy18Ali Ebrahim19Julien Orlans20Selina L. S. Storm21Tiankun Zhou22Shigeki Owada23Rie Tanaka24Kensuke Tono25Gwyndaf Evans26Robin L. Owen27Frances A. Houle28Nicholas K. Sauter29Christopher J. Schofield30James Spencer31Vittal K. Yachandra32Junko Yano33Jan F. Kern34Allen M. Orville35Diamond Light Source, Harwell Science and Innovation CampusMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryDiamond Light Source, Harwell Science and Innovation CampusSchool of Cellular and Molecular Medicine, University of Bristol, University WalkMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryPolyPico Technologies Ltd, Unit 10, Airways Technology Park, Rathmacullig WestSchool of Cellular and Molecular Medicine, University of Bristol, University WalkMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryDiamond Light Source, Harwell Science and Innovation CampusDepartment of Chemistry, Chemistry Research Laboratory, University of OxfordDepartment of Chemistry, Chemistry Research Laboratory, University of OxfordDepartment of Chemistry, Chemistry Research Laboratory, University of OxfordDepartment of Chemistry, Chemistry Research Laboratory, University of OxfordDiamond Light Source, Harwell Science and Innovation CampusDiamond Light Source, Harwell Science and Innovation CampusDiamond Light Source, Harwell Science and Innovation CampusDiamond Light Source, Harwell Science and Innovation CampusDiamond Light Source, Harwell Science and Innovation CampusDiamond Light Source, Harwell Science and Innovation CampusDiamond Light Source, Harwell Science and Innovation CampusRIKEN SPring-8 CenterRIKEN SPring-8 CenterRIKEN SPring-8 CenterDiamond Light Source, Harwell Science and Innovation CampusDiamond Light Source, Harwell Science and Innovation CampusChemical Sciences Division, Lawrence Berkeley National LaboratoryMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryDepartment of Chemistry, Chemistry Research Laboratory, University of OxfordSchool of Cellular and Molecular Medicine, University of Bristol, University WalkMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National LaboratoryDiamond Light Source, Harwell Science and Innovation CampusCurrently many of the time resolved serial femtosecond (SFX) crystallography experiments are done with light driven protein systems, whereas the reaction initiation for non-light triggered enzymes remains a major bottle neck. Here, the authors present an expanded Drop-on-Tape system, where picoliter-sized droplets of a substrate or inhibitor are turbulently mixed with nanoliter sized droplets of microcrystal slurries, and they use it for time-resolved SFX measurements of inhibitor binding to lysozyme and secondly, binding of a β-lactam antibiotic to a bacterial serine β-lactamase.https://doi.org/10.1038/s41467-021-24757-7 |
| spellingShingle | Agata Butryn Philipp S. Simon Pierre Aller Philip Hinchliffe Ramzi N. Massad Gabriel Leen Catherine L. Tooke Isabel Bogacz In-Sik Kim Asmit Bhowmick Aaron S. Brewster Nicholas E. Devenish Jürgen Brem Jos J. A. G. Kamps Pauline A. Lang Patrick Rabe Danny Axford John H. Beale Bradley Davy Ali Ebrahim Julien Orlans Selina L. S. Storm Tiankun Zhou Shigeki Owada Rie Tanaka Kensuke Tono Gwyndaf Evans Robin L. Owen Frances A. Houle Nicholas K. Sauter Christopher J. Schofield James Spencer Vittal K. Yachandra Junko Yano Jan F. Kern Allen M. Orville An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography Nature Communications |
| title | An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography |
| title_full | An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography |
| title_fullStr | An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography |
| title_full_unstemmed | An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography |
| title_short | An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography |
| title_sort | on demand drop on drop method for studying enzyme catalysis by serial crystallography |
| url | https://doi.org/10.1038/s41467-021-24757-7 |
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