| 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
|
s, nm-1
|
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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