| MWexperimental | 17 | kDa |
| MWexpected | 11 | kDa |
| VPorod | 30 | nm3 |
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log I(s)
1.16×103
1.16×102
1.16×101
1.16×100
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s, nm-1
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Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements.
Fuertes G Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA, Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017) Europe PMCSASDER2 – Unlabeled Importin Beta Binding domain (IBB) from importin subunit alpha-1 without denaturant
Importin subunit alpha-1|
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Fits and models
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Rg, nm
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Synchrotron SAXS
data from solutions of
Unlabeled Importin Beta Binding domain (IBB) from importin subunit alpha-1 without denaturant
in
PBS, 10 mM DTT, pH 7.4
were collected
on the
EMBL P12 beam line
at the PETRA III storage ring
(DESY; Hamburg, Germany)
using a Pilatus 2M detector
at a sample-detector distance of 3 m and
at a wavelength of λ = 0.1 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
Solute concentrations ranging between 1 and 5 mg/ml were measured
at 23°C.
20 successive
0.050 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.
The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
The protein contains a penultimate non-canonical amino acid p-acetylphenylalanine (207 Da) that is represented as U (selenocysteine, 168 Da) in the amino acid sequence for the entry. Therefore, the calculated MW from sequence (MW(expected)) must be adjusted accordingly (ca. 40 Da).
Tags:
idp
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