A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins.

Yu M, Gruzinov AY, Ruan H, Scheidt T, Chowdhury A, Giofrè S, Mohammed ASA, Caria J, Sauter PF, Svergun DI, Lemke EA, Proc Natl Acad Sci U S A 121(50):e2415220121 (2024) Europe PMC

SASDUS9 – Wild-type Elastin-like Polypeptide (ELP) in 0.5 M Urea

Elastin-like polypeptide
MWexperimental 21 kDa
MWexpected 13 kDa
VPorod 47 nm3
log I(s) 4.68×10-3 4.68×10-4 4.68×10-5 4.68×10-6
Elastin-like polypeptide small angle scattering data  s, nm-1
ln I(s)
Elastin-like polypeptide Guinier plot ln 4.69×10-3 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Elastin-like polypeptide Kratky plot 1.104 0 3 sRg
p(r)
Elastin-like polypeptide pair distance distribution function Rg: 3.2 nm 0 Dmax: 10.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of wild-type ELP in phosphate buffered saline containing 0.5 M urea, 0.3 M KCl, 5 mM DTT, pH 7.4 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.092 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 20.00 μl sample at 20 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column at 20°C. 2400 successive 0.250 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.

Wild-type ELP in 0.5 M urea measured at 13428 eV. SAXS data measured at several different energies spanning the K-absorbtion edge of bromine are made available in the full entry zip archive.

Elastin-like polypeptide (Wild-type ELP)
Mol. type   Protein
Organism   synthetic construct
Olig. state   Monomer
Mon. MW   13.1 kDa
Sequence   FASTA