Dmax unknown – experimental data range validation not possible.
There are no models related to this curve.
Synchrotron SAXS data from solutions of ground Doryteuthis squid lens (100% layer) diluted in phosphate buffered saline, pH 7, were collected on the X9A camera on the storage ring National Synchrotron Light Source (NSLS; Brookhaven, NY, USA) using a 20Hz Pilatus 300K detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsin θ/λ and 2θ is the scattering angle). The data were normalized to the intensity of the transmitted beam and radially averaged, and the scattering of the solvent blank (PBS) was subtracted from the diluted lens data. The dataset shown in this entry was collected from a suspension containing about 18 mg/ml of lens protein (refer to the full entry zip archive for the complete dilution series of 9, 4.5, 2.25, 1.13, 0.56, 0.28, 0.14 and 0.07 mg/ml lens protein). The lens contains about 40 unique S-crystallins isoforms that vary in molecular weight due to length variation in a disordered region encoded in the central exon of the coding sequence such that loops form protruding from the folded protein. S-crystallins are dimeric and globular, such that each dimer has two of these disordered loops, which form linking structures between particles in the system. The full set of sequences describing the protein polydispersity in this system is available at GenBank BioProject PRJNA386124.
Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN. Concentration = UNKNOWN
s, nm-1
