Nature Communications (Jul 2021)
An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography
- 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
Affiliations
- Agata Butryn
- Diamond Light Source, Harwell Science and Innovation Campus
- Philipp S. Simon
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Pierre Aller
- Diamond Light Source, Harwell Science and Innovation Campus
- Philip Hinchliffe
- School of Cellular and Molecular Medicine, University of Bristol, University Walk
- Ramzi N. Massad
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Gabriel Leen
- PolyPico Technologies Ltd, Unit 10, Airways Technology Park, Rathmacullig West
- Catherine L. Tooke
- School of Cellular and Molecular Medicine, University of Bristol, University Walk
- Isabel Bogacz
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- In-Sik Kim
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Asmit Bhowmick
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Aaron S. Brewster
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Nicholas E. Devenish
- Diamond Light Source, Harwell Science and Innovation Campus
- Jürgen Brem
- Department of Chemistry, Chemistry Research Laboratory, University of Oxford
- Jos J. A. G. Kamps
- Department of Chemistry, Chemistry Research Laboratory, University of Oxford
- Pauline A. Lang
- Department of Chemistry, Chemistry Research Laboratory, University of Oxford
- Patrick Rabe
- Department of Chemistry, Chemistry Research Laboratory, University of Oxford
- Danny Axford
- Diamond Light Source, Harwell Science and Innovation Campus
- John H. Beale
- Diamond Light Source, Harwell Science and Innovation Campus
- Bradley Davy
- Diamond Light Source, Harwell Science and Innovation Campus
- Ali Ebrahim
- Diamond Light Source, Harwell Science and Innovation Campus
- Julien Orlans
- Diamond Light Source, Harwell Science and Innovation Campus
- Selina L. S. Storm
- Diamond Light Source, Harwell Science and Innovation Campus
- Tiankun Zhou
- Diamond Light Source, Harwell Science and Innovation Campus
- Shigeki Owada
- RIKEN SPring-8 Center
- Rie Tanaka
- RIKEN SPring-8 Center
- Kensuke Tono
- RIKEN SPring-8 Center
- Gwyndaf Evans
- Diamond Light Source, Harwell Science and Innovation Campus
- Robin L. Owen
- Diamond Light Source, Harwell Science and Innovation Campus
- Frances A. Houle
- Chemical Sciences Division, Lawrence Berkeley National Laboratory
- Nicholas K. Sauter
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Christopher J. Schofield
- Department of Chemistry, Chemistry Research Laboratory, University of Oxford
- James Spencer
- School of Cellular and Molecular Medicine, University of Bristol, University Walk
- Vittal K. Yachandra
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Junko Yano
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Jan F. Kern
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Allen M. Orville
- Diamond Light Source, Harwell Science and Innovation Campus
- DOI
- https://doi.org/10.1038/s41467-021-24757-7
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 7
Abstract
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.
