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![[Figure 5]](rv5134fig5mag.jpg)
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Figure 5
Example scattering data calibrated to absolute intensity relative to water (0.0163 Å−1). (a) Instrument background, measured with no capillary at the sample position (grey) and with an empty capillary (black). (b) An extended bovine serum albumin (BSA) dilution series measured at concentrations of 6, 4, 2.6, 1.7, 1.2, 0.8, 0.5, 0.35. 0.2, 0.13 and 0.08 mg ml−1 from top to bottom. The inset shows the Guinier fitting and residuals for the 0.08 mg ml−1 sample. For each dilution, 20 × 1 s frames were measured from 30 µl samples of BSA in 50 mM Tris pH 7.5, 150 mM NaCl, 2% glycerol at 15°C. (c) An SEC-SAXS trace of BSA. Blue points plot the magnitude of the scattering signal defined as the ratio of each frame to a background frame. The radius of gyration (red) is shown calculated for individual frames with scattering signal above a threshold. The inset shows scattering data derived by averaging frames across the main peak. The data represent a 50 µl sample of BSA at 5 mg ml−1 run on a KW403 column (Shodex) at 0.16 ml min−1 with a similar running buffer as described for panel (b). |
![[Figure 5]](rv5134fig5.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
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