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

SASDMJ3 – Zinc-finger-associated domain from Drosophila Motif 1 binding protein (M1BP)

LD30467p (Motif 1 binding protein)
MWexperimental 23 kDa
MWexpected 22 kDa
VPorod 33 nm3
log I(s) 1.34×10-2 1.34×10-3 1.34×10-4 1.34×10-5
LD30467p (Motif 1 binding protein) small angle scattering data  s, nm-1
ln I(s)
LD30467p (Motif 1 binding protein) Guinier plot ln 1.34×10-2 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
LD30467p (Motif 1 binding protein) Kratky plot 1.104 0 √3 sRg
p(r)
LD30467p (Motif 1 binding protein) pair distance distribution function Rg: 2.4 nm 0 Dmax: 9.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
LD30467p (Motif 1 binding protein) OTHER model
Synchrotron SAXS data from solutions of the zinc-finger-associated domain from Drosophila Motif 1 binding protein (M1BP) in 20 mM Bis-Tris-Propane, 100 mM NaCl, 5 mM DTT, pH 8.5 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 5.20 mg/ml was measured at 20°C. 60 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

LD30467p (Motif 1 binding protein) (M1BP)
Mol. type   Protein
Organism   Drosophila melanogaster
Olig. state   Dimer
Mon. MW   11.2 kDa
 
UniProt   Q9VHM3 (1-98)
Sequence   FASTA