Development of serial X-ray fluorescence holography for radiation-sensitive protein crystals

open access.

Bibliographische Detailangaben
Veröffentlicht in:Journal of synchrotron radiation. - 1994. - 30(2023), Pt 2 vom: 01. März, Seite 368-378
1. Verfasser: Ang, Artoni Kevin R (VerfasserIn)
Weitere Verfasser: Umena, Yasufumi, Sato-Tomita, Ayana, Shibayama, Naoya, Happo, Naohisa, Marumi, Riho, Yamamoto, Yuta, Kimura, Koji, Kawamura, Naomi, Takano, Yu, Matsushita, Tomohiro, Sasaki, Yuji C, Shen, Jian Ren, Hayashi, Kouichi
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:Journal of synchrotron radiation
Schlagworte:Journal Article X-ray fluorescence holography atomic structures protein structures Proteins
Beschreibung
Zusammenfassung:open access.
X-ray fluorescence holography (XFH) is a powerful atomic resolution technique capable of directly imaging the local atomic structure around atoms of a target element within a material. Although it is theoretically possible to use XFH to study the local structures of metal clusters in large protein crystals, the experiment has proven difficult to perform, especially on radiation-sensitive proteins. Here, the development of serial X-ray fluorescence holography to allow the direct recording of hologram patterns before the onset of radiation damage is reported. By combining a 2D hybrid detector and the serial data collection used in serial protein crystallography, the X-ray fluorescence hologram can be directly recorded in a fraction of the measurement time needed for conventional XFH measurements. This approach was demonstrated by obtaining the Mn Kα hologram pattern from the protein crystal Photosystem II without any X-ray-induced reduction of the Mn clusters. Furthermore, a method to interpret the fluorescence patterns as real-space projections of the atoms surrounding the Mn emitters has been developed, where the surrounding atoms produce large dark dips along the emitter-scatterer bond directions. This new technique paves the way for future experiments on protein crystals that aim to clarify the local atomic structures of their functional metal clusters, and for other related XFH experiments such as valence-selective XFH or time-resolved XFH
Beschreibung:Date Completed 10.03.2023
Date Revised 14.09.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1600-5775
DOI:10.1107/S1600577522011833