Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions

Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B, The EMBO Journal (2022) DOI

SASDKV4 – Teneurin-4 dimer mutant in SEC buffer (20 mM HEPES, 150 mM NaCl)

Teneurin-4 (S2585C)

MW^experimental	600	kDa
MW^expected	537	kDa
V^Porod	1260	nm³

log I(s) 5.19×10^-1 5.19×10^-2 5.19×10^-3 5.19×10^-4

Teneurin-4 (S2585C) small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 5.20×10^-1 R_g: 7.1 nm 0 (7.1 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 7.4 nm 0 D_max: 29.5 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

0.969
0.749

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Teneurin-4 dimer mutant in SEC buffer (20 mM HEPES, 150 mM NaCl) Rg histogram

R_g, nm

Synchrotron SAXS data from solutions of mutant Teneurin-4 (S2585C) in 20 mM HEPES, 150 mM NaCl, pH 7.8 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.5 m and (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 20°C. 25 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.

X-ray wavelength: UNKNOWN

Teneurin-4 (S2585C) (TENM4 S2585C)
Mol. type		Protein
Organism		Homo sapiens
Olig. state		Dimer
Mon. MW		268.4 kDa

UniProt		Q6N022 (373-2769)
Sequence		FASTA