Structural insights into highly similar spatial organization of zinc-finger associated domains with a very low sequence similarity.

Bonchuk AN, Boyko KM, Nikolaeva AY, Burtseva AD, Popov VO, Georgiev PG, Structure (2022) Europe PMC

SASDMG3 – Tetrameric zinc-finger associated domain of Drosophila Pita protein

LD15650p (Pita, isoform A)

MW^experimental	53	kDa
MW^expected	52	kDa
V^Porod	62	nm³

log I(s) 2.97×10^-2 2.97×10^-3 2.97×10^-4 2.97×10^-5

LD15650p (Pita, isoform A) small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 2.98×10^-2 R_g: 2.4 nm 0 (2.4 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 2.4 nm 0 D_max: 7.6 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.6

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.478
0.750

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from solutions of tetrameric zinc-finger associated domain of Drosophila Pita protein in 20 mM Tris, 100 mM NaCl, 5 mM DTT, pH 7.4 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.70 mg/ml was measured at 10.3°C. 30 successive 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.

Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN

LD15650p (Pita, isoform A) (Pita)
Mol. type		Protein
Organism		Drosophila melanogaster
Olig. state		Tetramer
Mon. MW		13.0 kDa

UniProt		Q95RQ8 (1-111)
Sequence		FASTA