Time-resolved small-angle X-ray scattering system development for the biological macromolecules at SACLA: A pilot study
A time-resolved small-angle X-ray scattering (SAXS) system for protein solution samples using an X-ray free-electron laser (XFEL) was established by developing a SAXS diffractometer by integrating a helium path into the DAPHNIS system initially designed for Serial Femtosecond Crystallography (SFX) experiments at BL2 of SACLA. This modification enabled us to successfully capture the SAXS profiles of ovalbumin under conditions without any reaction trigger, using both the newly developed system and the sample solution flow device that was originally designed for SFX experiments. Furthermore, we conducted acid denaturation experiments on cytochrome c, using a T-junction-type solution mixing flow system, and observed the denaturation-induced changes in the SAXS profiles.
Authors
- So Iwata (ORCID: https://orcid.org/0000-0003-1735-2937)
- Eriko Nango (ORCID: https://orcid.org/0000-0001-9851-7355)
- Tomoyuki Tanaka (ORCID: https://orcid.org/0000-0002-9886-5947)
- Fangjia Luo (ORCID: https://orcid.org/0000-0003-0631-6236)
- Kensuke Tono (ORCID: https://orcid.org/0000-0003-1218-3759)
- Keiko Yatabe
- Nobutaka Shimizu (ORCID: https://orcid.org/0000-0002-3636-1663)
Institutions
- High Energy Accelerator Research Organization (JP)
- Tohoku University (JP)
- Kyoto University (JP)
- SPring-8 (JP)
- Japan Synchrotron Radiation Research Institute (JP)
Publication Details
- Journal
- Biophysics and Physicobiology
- Published
- 2025-01-01
- DOI
- https://doi.org/10.2142/biophysico.bppb-v22.0007
- Primary Topic
- Enzyme Structure and Function
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Japan Agency for Medical Research and Development
- Japan Society for the Promotion of Science
- RIKEN