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...
Guardado en:
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/55ce2079723b464484f4eed86828b06d |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:55ce2079723b464484f4eed86828b06d |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:55ce2079723b464484f4eed86828b06d2021-12-02T17:57:04ZAn on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography10.1038/s41467-021-24757-72041-1723https://doaj.org/article/55ce2079723b464484f4eed86828b06d2021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24757-7https://doaj.org/toc/2041-1723Currently 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.Agata ButrynPhilipp S. SimonPierre AllerPhilip HinchliffeRamzi N. MassadGabriel LeenCatherine L. TookeIsabel BogaczIn-Sik KimAsmit BhowmickAaron S. BrewsterNicholas E. DevenishJürgen BremJos J. A. G. KampsPauline A. LangPatrick RabeDanny AxfordJohn H. BealeBradley DavyAli EbrahimJulien OrlansSelina L. S. StormTiankun ZhouShigeki OwadaRie TanakaKensuke TonoGwyndaf EvansRobin L. OwenFrances A. HouleNicholas K. SauterChristopher J. SchofieldJames SpencerVittal K. YachandraJunko YanoJan F. KernAllen M. OrvilleNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-7 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Science Q |
spellingShingle |
Science Q 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 |
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. |
format |
article |
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 |
title |
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_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_sort |
on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/55ce2079723b464484f4eed86828b06d |
work_keys_str_mv |
AT agatabutryn anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT philippssimon anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT pierrealler anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT philiphinchliffe anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT ramzinmassad anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT gabrielleen anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT catherineltooke anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT isabelbogacz anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT insikkim anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT asmitbhowmick anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT aaronsbrewster anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT nicholasedevenish anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT jurgenbrem anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT josjagkamps anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT paulinealang anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT patrickrabe anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT dannyaxford anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT johnhbeale anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT bradleydavy anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT aliebrahim anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT julienorlans anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT selinalsstorm anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT tiankunzhou anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT shigekiowada anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT rietanaka anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT kensuketono anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT gwyndafevans anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT robinlowen anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT francesahoule anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT nicholasksauter anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT christopherjschofield anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT jamesspencer anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT vittalkyachandra anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT junkoyano anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT janfkern anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT allenmorville anondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT agatabutryn ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT philippssimon ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT pierrealler ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT philiphinchliffe ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT ramzinmassad ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT gabrielleen ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT catherineltooke ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT isabelbogacz ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT insikkim ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT asmitbhowmick ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT aaronsbrewster ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT nicholasedevenish ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT jurgenbrem ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT josjagkamps ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT paulinealang ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT patrickrabe ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT dannyaxford ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT johnhbeale ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT bradleydavy ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT aliebrahim ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT julienorlans ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT selinalsstorm ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT tiankunzhou ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT shigekiowada ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT rietanaka ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT kensuketono ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT gwyndafevans ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT robinlowen ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT francesahoule ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT nicholasksauter ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT christopherjschofield ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT jamesspencer ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT vittalkyachandra ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT junkoyano ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT janfkern ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography AT allenmorville ondemanddropondropmethodforstudyingenzymecatalysisbyserialcrystallography |
_version_ |
1718379045057462272 |