期刊
JOURNAL OF APPLIED CRYSTALLOGRAPHY
卷 55, 期 -, 页码 340-352出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600576722001923
关键词
small-angle X-ray scattering; wide-angle X-ray scattering; SAXS-WAXS; SWAXS; online size exclusion chromatography; integrated UV-Vis absorption and refractometry; biomolecular solution scattering
资金
- Academia Sinica, Taiwan Protein Project
- Taiwan Ministry of Science and Technology through a Flagship Project [10773FS13]
Recent developments in instrumentation and data analysis have made biological small-angle X-ray scattering (BioSAXS) a mature and popular tool in structural biology. This article reports on an advanced endstation developed for biological SAXS-WAXS at Taiwan Photon Source, featuring an in-vacuum detection system and an online size-exclusion chromatography system. The endstation allows high-throughput biomolecular conformation and composition determinations.
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 similar to 0.005-2.0 angstrom(-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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据