Structure of SALL4 zinc finger domain reveals link between AT-rich DNA binding and Okihiro syndrome.

Watson JA, Pantier R, Jayachandran U, Chhatbar K, Alexander-Howden B, Kruusvee V, Prendecki M, Bird A, Cook AG, Life Sci Alliance 6(3) (2023) Europe PMC

SASDP64 – SALL4 Zinc Finger Cluster 4

Sal-like protein 4
MWexperimental 8 kDa
MWexpected 8 kDa
VPorod 11 nm3
log I(s) 8.19×10-3 8.19×10-4 8.19×10-5 8.19×10-6
Sal-like protein 4 small angle scattering data  s, nm-1
ln I(s)
Sal-like protein 4 Guinier plot ln 8.19×10-3 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Sal-like protein 4 Kratky plot 1.104 0 √3 sRg
p(r)
Sal-like protein 4 pair distance distribution function Rg: 2.0 nm 0 Dmax: 5.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Sal-like protein 4 DAMMIN model
log I(s)
 s, nm-1
Sal-like protein 4 OTHER model
Synchrotron SAXS data from solutions of the SALL4 zinc finger cluster 4 in 20 mM Tris-HCl, pH 7.5, 200 mM NaCl, were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 6.7 mg/ml was injected at a 0.10 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 22°C. 619 successive 3 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.

The ATSAS 3.0.5 suite of software was used for processing data (Manalastas-Cantos, et al. 2021).

Sal-like protein 4 (SALL4)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   8.4 kDa
 
UniProt   Q8BX22 (870-940)
Sequence   FASTA