Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody.

Covaceuszach S, Cassetta A, Konarev PV, Gonfloni S, Rudolph R, Svergun DI, Lamba D, Cattaneo A, J Mol Biol 381(4):881-96 (2008) Europe PMC

SASDAS5 – ad11 Fab

aD11 Fab

MW^experimental	50	kDa
MW^expected	50	kDa
V^Porod	95	nm³

log I(s) 1.03×10⁶ 1.03×10⁵ 1.03×10⁴ 1.03×10³

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 1.03×10⁶ R_g: 2.6 nm 0 (2.6 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 2.6 nm 0 D_max: 8 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.2

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.116
3.201

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from solutions of ad11 Fab in 50 mM Na-phosphate 1mM ethylenediaminetetraacetic aci, pH 7 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). at 15°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN. Concentration = UNKNOWN

Tags: X33

aD11 Fab (Fab)
Mol. type		Protein
Organism		Mus musculus
Olig. state		Dimer
Mon. MW		25 kDa
Sequence		FASTA