Crystal structure of the adipokine isthmin-1 reveals an unusual fold

Tongqing Li.

SASDVX6 – Monomeric Adhesion-associated domain in MUC4 and Other Proteins (AMOP-domain) of Isthmin-1, I455E, F458E douple mutant

L-AMOP-IFEE
MWexperimental 30 kDa
MWexpected 25 kDa
VPorod 46874 nm3
log I(s) 1.30×10-1 1.30×10-2 1.30×10-3 1.30×10-4
L-AMOP-IFEE small angle scattering data  s, nm-1
ln I(s)
L-AMOP-IFEE Guinier plot ln 1.31×10-1 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
L-AMOP-IFEE Kratky plot 1.104 0 √3 sRg
p(r)
L-AMOP-IFEE pair distance distribution function Rg: 2.5 nm 0 Dmax: 8.8 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of Monomeric Adhesion-associated domain in MUC4 and Other Proteins (AMOP-domain) of Isthmin-1, I455E, F458E douple mutant in 20 mM HEPES 100 mM NaCl, pH 7.5 were collected using a Rigaku HyPix-3000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.1542 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 4°C. Nine successive 600 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.

L-AMOP-IFEE
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   24.8 kDa
 
UniProt   B1AKI9 (263-464)
Sequence   FASTA