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![[Figure 4]](tj5032fig4mag.jpg)
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Figure 4
A standard protein mixture analysed using SEC–SANS. (a) and (b) Chromatograms at 280 nm (red) and scattergrams at Q < 0.03 Å−1 (blue) of 200 µl of a standard protein mix (7 mg ml−1) injected on a Superdex 200 (10/300) column, eluted at 0.15 ml min−1 and measured using a neutron wavelength of 6 Å with a spread of (a) 10% or (b) 20%. (c) Scattering curves extracted from the first chromatogram peak (red, thyroglobulin, 330 s exposure), the second peak (blue, γ-globulin, 120 s exposure) and the third peak [green, ovalbumin, 150 s exposure, black arrow in panel (a)]. Continuous lines represent data recorded using the standard 10% wavelength spread, while dotted lines represent data recorded using a 20% wavelength spread `high flux' option. The continuous black line shows the theoretical curve calculated using Pepsi-SANS (Grudinin et al., 2017  ) from the structure of ovalbumin (PDB ID 1ova; Stein et al., 1991) at 0.35 mg ml−1 (42 750 kDa and ξ280nm = 31 400 M−1 cm−1). The data were reduced using GRASP and plotted using SANS reduction macros written by S. Kline (2006) for the Igor Pro software. |
![[Figure 4]](tj5032fig4.jpg)
 | JOURNAL OF APPLIED CRYSTALLOGRAPHY |
ISSN: 1600-5767
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