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. 2012 Jul 3;69(21):3701–3713. doi: 10.1007/s00018-012-1049-7

Table 2.

Structural parameters of the CFTR nucleotide binding domains in solution, obtained from SAXS experiments

Control 0 ATP +PBF 25 nM 2 mM ATP 2 mM ATP + PBF 25 nM
R g (nm) 2.71 ± 0.03 1.92 ± 0.07 2.11 ± 0.01 3.06 ± 0.05
I(0) 38,705 ± 33 19,958 ± 133 41,873 ± 86 28,818 ± 230
c (mg/ml) 1.68 1.72 1.80 1.23
MM (KDa) 64.50 ± 0.05 32.49 ± 0.23 65.13 ± 0.13 65.59 ± 0.52
R g* (nm) 2.78 ± 0.01 1.83 ± 0.01 2.20 ± 0.07 3.14 ± 0.03
D max (nm) 7.81 5.30 6.24 10.12

MM molecular mass calculated from the experimental data obtained from the extrapolation of the Guinier plot to the origin, I(0), and the protein concentration, c, relative to the scattering of 4.5 mg/ml bovine serum albumin [I(0) = 1,078,000]. R g gyration radius estimated from the slope of the Guinier plot. The maximum length of the particle D max was estimated from the distance distribution function, P(r), with an estimated gyration radius R g* obtained from the function