| MWexperimental | 97 | kDa |
| MWexpected | 97 | kDa |
| VPorod | 75 | nm3 |
|
log I(s)
2.61×101
2.61×100
2.61×10-1
2.61×10-2
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s, nm-1
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Single-engineered-residue solvation perturbations regulate global protein architecture and function.
Liu Y, Zhai J, Cao S, Guo H, Zhang H, Song B, Guo J, Men D, He X, Li D, Nat Commun (2026) Europe PMCSASDY97 – Alkaline phosphatase (ALP) under vis
Wild Alkaline Phosphatase under vis|
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Fits and models
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Synchrotron SAXS
data from solutions of
Alkaline phosphatase (ALP) under vis
in
25 mM Tris, 100 mM NaCl, 2 mM TCEP, 3% (w/v) glycerol, pH 7.5
were collected
on the
BL19U2 beam line
at the Shanghai Synchrotron Radiation Facility (SSRF) storage ring
(Shanghai, China)
using a Pilatus 1M detector
at a sample-detector distance of 2.6 m and
at a wavelength of λ = 0.1033 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 1.00 mg/ml was measured
at 20°C.
20 successive
0.200 second frames were collected.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
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