Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a)

Dimasi N, Roessle M, Moran O, Candiano G, Svergun D, Biassoni R, International Journal of Biological Macromolecules 40(3):193-200 (2007) DOI

SASDNB2 – Human NK inhibitory receptor IRp60 with an immunoglobulin-like fold

CMRF35-like molecule 8
MWexperimental 14 kDa
MWexpected 12 kDa
VPorod 22 nm3
log I(s) 1.92×101 1.92×100 1.92×10-1 1.92×10-2
CMRF35-like molecule 8 small angle scattering data  s, nm-1
ln I(s)
CMRF35-like molecule 8 Guinier plot ln 1.92×101 Rg: 2.0 nm 0 (2.0 nm)-2 s2
CMRF35-like molecule 8 Kratky plot 1.104 0 3 sRg
CMRF35-like molecule 8 pair distance distribution function Rg: 2.0 nm 0 Dmax: 7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
CMRF35-like molecule 8 PDB (PROTEIN DATA BANK) model

log I(s)
 s, nm-1
CMRF35-like molecule 8 DAMMIN model

Synchrotron SAXS data from solutions of Human NK inhibitory receptor IRp60 with an immunoglobulin-like fold in MES buffer with 3mM DTT, pH 5.5 were collected on the EMBL X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.4 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.50 mg/ml was measured at 8°C. One 180 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN

Tags: X33
CMRF35-like molecule 8 (IgV like V-type)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   11.7 kDa
UniProt   Q9UGN4 (19-123)
Sequence   FASTA