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Performance of the new biological small- and wide-angle X-ray scattering beamline 13A at the Taiwan Photon Source.
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.
Affiliation
  • Shih O; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Liao KF; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Yeh YQ; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Su CJ; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Wang CA; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Chang JW; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Wu WR; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Liang CC; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Lin CY; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Lee TH; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Chang CH; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Chiang LC; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Chang CF; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Liu DG; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Lee MH; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Liu CY; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Hsu TW; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Mansel B; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
  • Ho MC; Institute of Biochemical Sciences and Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei 11529, Taiwan.
  • Shu CY; Academia Sinica Grid Computing Centre, Academia Sinica, Nankang, Taipei 11529, Taiwan.
  • Lee F; Academia Sinica Grid Computing Centre, Academia Sinica, Nankang, Taipei 11529, Taiwan.
  • Yen E; Academia Sinica Grid Computing Centre, Academia Sinica, Nankang, Taipei 11529, Taiwan.
  • Lin TC; Department of Chemical Engineering, National Tsing Hua University, Hsinchu 30013, Taiwan.
  • Jeng U; National Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu 30076, Taiwan.
J Appl Crystallogr ; 55(Pt 2): 340-352, 2022 Apr 01.
Article in En | MEDLINE | ID: mdl-35497659
ABSTRACT
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: J Appl Crystallogr Year: 2022 Document type: Article Affiliation country: Taiwan
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Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: J Appl Crystallogr Year: 2022 Document type: Article Affiliation country: Taiwan