A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies.

Gurusaran M, Davies OR, Elife 10 (2021) Europe PMC

SASDJF5 – SUN domain of SUN1 harbouring mutation I673E - monomer

SUN domain-containing protein 1, I673E
MWexperimental 22 kDa
MWexpected 23 kDa
VPorod 42 nm3
log I(s) 4.20×10-2 4.20×10-3 4.20×10-4 4.20×10-5
SUN domain-containing protein 1, I673E small angle scattering data  s, nm-1
ln I(s)
SUN domain-containing protein 1, I673E Guinier plot ln 4.21×10-2 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
SUN domain-containing protein 1, I673E Kratky plot 1.104 0 √3 sRg
p(r)
SUN domain-containing protein 1, I673E pair distance distribution function Rg: 2.2 nm 0 Dmax: 8.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
SUN domain-containing protein 1, I673E PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
SUN domain-containing protein 1, I673E SREFLEX model
log I(s)
 s, nm-1
SUN domain-containing protein 1, I673E DAMMIF model
SUN domain-containing protein 1, I673E DAMMIF model
Synchrotron SAXS data from solutions of the SUN domain of SUN1 (I673E) in 20 mM Tris pH 8.0, 150 mM KCl, were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a wavelength of λ = 0.095 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 100.00 μl sample at 10 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 25 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

SUN domain-containing protein 1, I673E (SUN1, I673E)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   22.5 kDa
 
UniProt   O94901 (616-812)
Sequence   FASTA
 
PDB ID   6R15
 
PDB ID   6R15