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

SASDAU5 – ad11 Fab + NGF

aD11 Fab
NGF

MW^experimental	130	kDa
MW^expected	100	kDa
V^Porod	255	nm³

log I(s) 2.36×10⁶ 2.36×10⁵ 2.36×10⁴ 2.36×10³

aD11 Fab NGF small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 2.37×10⁶ R_g: 4.3 nm 0 (4.3 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 4.3 nm 0 D_max: 16 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.8

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.116
2.857

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 + NGF in 30 mM Na-phosphate 75 mM NaCl, 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. Two successive 120 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.

Wavelength = UNKNOWN. Sample detector distance = UNKNOWN. Concentration = UNKNOWN

Tags: X33

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

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