Dmax unknown – experimental data range validation not possible.
There are no models related to this curve.
This data set displays SAXS data measured from egg albumen of a hard-boiled chicken egg. The most abundant protein in the egg white is ovalbumin, but there are other proteins present as well. After hard boiling, the egg proteins completely unfolded, resulting in a white gel. Because the proteins strongly interact to form extended materials, the parameters Rg and monomer molecular weight do not apply to this sample. Similarly, because this is a measurement of intact biological tissue, there is no experimental buffer per se to subtract, and accordingly, raw data without buffer subtraction are reported here. The sample measurement (1 x 1800 s exposure) was performed at 10°C. Measurements used a rotating-anode system with Cu Kα radiation (λ = 0.1542 nm) from a Bruker-Nonius FR591 generator operated at 3.4 kW. Collimation was performed using circular pinholes and Osmic Max-Flux confocal optics. The scattered X-rays (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle) were collected using a Bruker Hi-Star area detector. Data were collected at sample−detector distances of 54 and 150 cm, and the data merged to create a single profile over the range q ∈ [0.08, 3.5] nm−1. To minimize background, an integral vacuum with a pressure of < 0.3 mbar was maintained along the entire flight path.
s, nm-1
