journal menu
![[Figure 3]](co5025fig3mag.jpg)
|
|
Figure 3
Merged SAXS/WAXS data collected at X9 (courtesy of Marc Allaire) from lysozyme solutions at nominal concentrations of 5 mg ml−1 (black) and 50 mg ml−1 (red). Solid lines and symbols represent data after scaling and after subtraction of buffer scattering (green), respectively. The corresponding volume fractions of lysozyme are 0.37% and 3.70%, based on the assumed protein density of 1.35 mg ml−1. Scaling was performed by simply matching sample and buffer scattering intensity near q = 2.0 Å−1. As a result, the background-subtracted intensity artificially approaches 0 at the same q. The curves are essentially parallel to each other on a log scale, indicating that the background-subtracted data are proportional to the sample concentration and therefore good background subtraction (the red dashed line is scaled down from the 50 mg ml−1 data by a factor of 9.5). The low-q data for the 50 mg ml−1 sample is apparently affected by the inter-particle structure factor, as shown in the Guinier plot in the inset. |
![[Figure 3]](co5025fig3.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
