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Research articles

ScienceAsia 48 (2022):ID 399-405 |doi: 10.2306/scienceasia1513-1874.2022.064

Quality of protein structural data and radiation damage estimation at beamline 1.3W: SAXS/WAXS

Nuntaporn Kamonsutthipaijita,*, Nongluk Yutaekoolb, Siriwat Soontranona, Supagorn Rugmaia

ABSTRACT:     Small Angle X-ray Scattering (SAXS) is a useful technique that can provide structural information in terms of size, shape, and multiple conformations of a protein sample and can also be used to reconstruct a three-dimensional structure in low resolution of a macromolecule. SAXS data were collected and analyzed from a set of nine proteins with MW ranging from 14 to 400 kDa whose crystal structures were available from the PDB. The crystallographic data are used to validate the accuracy of the structure obtained from the SAXS data. By comparing data from both techniques, they can provide good complementary structural information to each other. Interestingly, no radiation damage of protein samples was observed by X-ray exposure at Beamline 1.3W, Synchrotron Light Research Institute, Thailand. This was confirmed with the chromatography technique by comparing the purity of the protein samples before and after SAXS measurements. The absorbed dose of each protein sample has also been calculated to confirm that the value is low enough to prevent damage to the proteins. This experiment has shown that the beamline provides SAXS measurements suitable for the broad range of protein structures in a non-destructive way and benefits the research community especially in the field of biological macromolecules in Southeast Asia and the nearby countries.

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a Synchrotron Light Research Institute (Public Organization), Nakhon Ratchasima 30000 Thailand
b School of Biochemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000 Thailand

* Corresponding author, E-mail: nuntaporn@slri.or.th

Received 19 Oct 2021, Accepted 16 Jan 2022