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  Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization

Josts, I., Niebling, S., Gao, Y., Levantino, M., Tidowa, H., & Monteiroa, D. (2018). Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization. IUCrJ, 5(6), 667-672. doi:10.1107/S2052252518012149.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0002-7F79-9 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-0D87-3
Genre: Journal Article

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This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
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2018
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© IUCrJ
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https://dx.doi.org/10.1107/S2052252518012149 (Publisher version)
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 Creators:
Josts, I.1, 2, Author
Niebling, S.1, 3, Author
Gao, Y.2, 4, Author           
Levantino, M.5, 6, Author
Tidowa, H.1, 2, Author
Monteiroa, D.1, Author
Affiliations:
1The Hamburg Center for Ultrafast Imaging, University of Hamburg, ou_persistent22              
2The Department of Chemistry, The University of Hamburg, ou_persistent22              
3The Department of Physics, The University of Hamburg, ou_persistent22              
4International Max Planck Research School for Ultrafast Imaging & Structural Dynamics (IMPRS-UFAST), Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_2266714              
5ESRF, The European Synchrotron, ou_persistent22              
6The Department of Physics and Chemistry, The University of Palermo, ou_persistent22              

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Free keywords: biophysics; X-ray solution scattering; photocaging; structural biology
 Abstract: This work demonstrates a new method for investigating time-resolved structural changes in protein conformation and oligomerization via photocage-initiated time-resolved X-ray solution scattering by observing the ATP-driven dimerization of the MsbA nucleotide-binding domain. Photocaged small molecules allow the observation of single-turnover reactions of non-naturally photoactivatable proteins. The kinetics of the reaction can be derived from changes in X-ray scattering associated with ATP-binding and subsequent dimerization. This method can be expanded to any small-molecule-driven protein reaction with conformational changes traceable by X-ray scattering where the small molecule can be photocaged.

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Language(s): eng - English
 Dates: 2018-05-212018-08-272018-11
 Publication Status: Published online
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S2052252518012149
 Degree: -

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Title: IUCrJ
Source Genre: Journal
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Publ. Info: Chester CH1 2HU, England : International Union of Crystallography (IUCr)
Pages: 6 Volume / Issue: 5 (6) Sequence Number: - Start / End Page: 667 - 672 Identifier: ISSN: 2052-2525
CoNE: https://pure.mpg.de/cone/journals/resource/2052-2525