Abstract
Recent improvements in X-ray detectors and synchrotron light sources have made it possible to measure time-resolved small-angle X-ray scattering (TR-SAXS) at millisecond time resolution. As an example, in this chapter we describe the beamline setup, experimental scheme, and the points that should be noted in stopped-flow TR-SAXS experiments for investigating the ferritin assembly reaction.
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Acknowledgments
The synchrotron radiation SAXS experiments were performed at BL45XU of SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute, Hyogo, Japan (proposals 2011A1133, 2012A1217, 2012B1114, 2013B1392, 2015A1374, 2016B1217, 2017A1403, 2017B1308, 2018A1262, and 2018B1404). This research was supported in part by the Platform for Drug Discovery, Information, and Structural Life Science of the Ministry of Education, Culture, Sports, Science and Technology of Japan.
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Sato, D., Hikima, T., Ikeguchi, M. (2023). Time-Resolved Small-Angle X-Ray Scattering of Protein Cage Assembly. In: Ueno, T., Lim, S., Xia, K. (eds) Protein Cages. Methods in Molecular Biology, vol 2671. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3222-2_12
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DOI: https://doi.org/10.1007/978-1-0716-3222-2_12
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