Real-time structural characterization of protein response to a caged compound by fast detector readout and high-brilliance synchrotron radiation
(2024) In Structure 32(9). p.3-1527- Abstract
Protein dynamics are essential to biological function, and methods to determine such structural rearrangements constitute a frontier in structural biology. Synchrotron radiation can track real-time protein dynamics, but accessibility to dedicated high-flux single X-ray pulse time-resolved beamlines is scarce and protein targets amendable to such characterization are limited. These limitations can be alleviated by triggering the reaction by laser-induced activation of a caged compound and probing the structural dynamics by fast-readout detectors. In this work, we established time-resolved X-ray solution scattering (TR-XSS) at the CoSAXS beamline at the MAX IV Laboratory synchrotron. Laser-induced activation of caged ATP initiated... (More)
Protein dynamics are essential to biological function, and methods to determine such structural rearrangements constitute a frontier in structural biology. Synchrotron radiation can track real-time protein dynamics, but accessibility to dedicated high-flux single X-ray pulse time-resolved beamlines is scarce and protein targets amendable to such characterization are limited. These limitations can be alleviated by triggering the reaction by laser-induced activation of a caged compound and probing the structural dynamics by fast-readout detectors. In this work, we established time-resolved X-ray solution scattering (TR-XSS) at the CoSAXS beamline at the MAX IV Laboratory synchrotron. Laser-induced activation of caged ATP initiated phosphoryl transfer in the adenylate kinase (AdK) enzyme, and the reaction was monitored up to 50 ms with a 2-ms temporal resolution achieved by the detector readout. The time-resolved structural signal of the protein showed minimal radiation damage effects and excellent agreement to data collected by a single X-ray pulse approach.
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- author
- Magkakis, Konstantinos ; Orädd, Fredrik ; Ahn, Byungnam LU ; Da Silva, Vanessa ; Appio, Roberto LU ; Plivelic, Tomás S. LU and Andersson, Magnus
- organization
- publishing date
- 2024-09-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- protein dynamics, synchrotron radiation, time-resolved X-ray solution scattering
- in
- Structure
- volume
- 32
- issue
- 9
- pages
- 3 - 1527
- publisher
- Cell Press
- external identifiers
-
- scopus:85198175960
- pmid:38889721
- ISSN
- 0969-2126
- DOI
- 10.1016/j.str.2024.05.015
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © 2024 The Author(s)
- id
- 66f8651f-a919-44e7-87a4-43097515f148
- date added to LUP
- 2024-11-27 11:42:28
- date last changed
- 2025-07-10 06:23:04
@article{66f8651f-a919-44e7-87a4-43097515f148,
abstract = {{<p>Protein dynamics are essential to biological function, and methods to determine such structural rearrangements constitute a frontier in structural biology. Synchrotron radiation can track real-time protein dynamics, but accessibility to dedicated high-flux single X-ray pulse time-resolved beamlines is scarce and protein targets amendable to such characterization are limited. These limitations can be alleviated by triggering the reaction by laser-induced activation of a caged compound and probing the structural dynamics by fast-readout detectors. In this work, we established time-resolved X-ray solution scattering (TR-XSS) at the CoSAXS beamline at the MAX IV Laboratory synchrotron. Laser-induced activation of caged ATP initiated phosphoryl transfer in the adenylate kinase (AdK) enzyme, and the reaction was monitored up to 50 ms with a 2-ms temporal resolution achieved by the detector readout. The time-resolved structural signal of the protein showed minimal radiation damage effects and excellent agreement to data collected by a single X-ray pulse approach.</p>}},
author = {{Magkakis, Konstantinos and Orädd, Fredrik and Ahn, Byungnam and Da Silva, Vanessa and Appio, Roberto and Plivelic, Tomás S. and Andersson, Magnus}},
issn = {{0969-2126}},
keywords = {{protein dynamics; synchrotron radiation; time-resolved X-ray solution scattering}},
language = {{eng}},
month = {{09}},
number = {{9}},
pages = {{3--1527}},
publisher = {{Cell Press}},
series = {{Structure}},
title = {{Real-time structural characterization of protein response to a caged compound by fast detector readout and high-brilliance synchrotron radiation}},
url = {{http://dx.doi.org/10.1016/j.str.2024.05.015}},
doi = {{10.1016/j.str.2024.05.015}},
volume = {{32}},
year = {{2024}},
}