Cargando…

Performance of the new biological small- and wide-angle X-ray scattering beamline 13A at the Taiwan Photon Source

Recent developments in the instrumentation and data analysis of synchrotron small-angle X-ray scattering (SAXS) on biomolecules in solution have made biological SAXS (BioSAXS) a mature and popular tool in structural biology. This article reports on an advanced endstation developed at beamline 13A of...

Descripción completa

Detalles Bibliográficos
Autores principales: Shih, O., Liao, K.-F., Yeh, Y.-Q., Su, C.-J., Wang, C.-A., Chang, J.-W., Wu, W.-R., Liang, C.-C., Lin, C.-Y., Lee, T.-H., Chang, C.-H., Chiang, L.-C., Chang, C.-F., Liu, D.-G., Lee, M.-H., Liu, C.-Y., Hsu, T.-W., Mansel, B., Ho, M.-C., Shu, C.-Y., Lee, F., Yen, E., Lin, T.-C., Jeng, U.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8985603/
https://www.ncbi.nlm.nih.gov/pubmed/35497659
http://dx.doi.org/10.1107/S1600576722001923
Descripción
Sumario:Recent developments in the instrumentation and data analysis of synchrotron small-angle X-ray scattering (SAXS) on biomolecules in solution have made biological SAXS (BioSAXS) a mature and popular tool in structural biology. This article reports on an advanced endstation developed at beamline 13A of the 3.0 GeV Taiwan Photon Source for biological small- and wide-angle X-ray scattering (SAXS–WAXS or SWAXS). The endstation features an in-vacuum SWAXS detection system comprising two mobile area detectors (Eiger X 9M/1M) and an online size-exclusion chromatography system incorporating several optical probes including a UV–Vis absorption spectrometer and refractometer. The instrumentation and automation allow simultaneous SAXS–WAXS data collection and data reduction for high-throughput biomolecular conformation and composition determinations. The performance of the endstation is illustrated with the SWAXS data collected for several model proteins in solution, covering a scattering vector magnitude q across three orders of magnitude. The crystal-model fittings to the data in the q range ∼0.005–2.0 Å(−1) indicate high similarity of the solution structures of the proteins to their crystalline forms, except for some subtle hydration-dependent local details. These results open up new horizons of SWAXS in studying correlated local and global structures of biomolecules in solution.