Design and structural characterisation of olfactomedin-1 variants as tools for functional studies.

Pronker MF, van den Hoek H, Janssen BJC, BMC Mol Cell Biol 20(1):50 (2019) Europe PMC

SASDF96 – Olfactomedin-1 BMY isoform

Noelin
MWI(0) 84 kDa
MWexpected 72 kDa
VPorod 160 nm3
log I(s) 8.40×101 8.40×100 8.40×10-1 8.40×10-2
Noelin small angle scattering data  s, nm-1
ln I(s)
Noelin Guinier plot ln 8.40×101 Rg: 5.4 nm 0 (5.4 nm)-2 s2
(sRg)2I(s)/I(0)
Noelin Kratky plot 1.104 0 √3 sRg
p(r)
Noelin pair distance distribution function Rg: 5.3 nm 0 Dmax: 16.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Noelin DAMMIF model
Synchrotron SAXS data from solutions of Olfactomedin-1 BMY isoform in 150 mM NaCl, 20 mM HEPES, pH 7.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09919 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.61 mg/ml was measured at 4°C. 10 successive 1 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.

Noelin (Olfm1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Tetramer
Mon. MW   18 kDa
 
UniProt   O88998-2 (17-153)
Sequence   FASTA