Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21.

Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J, PLoS One 10(8):e0136969 (2015) Europe PMC

SASDAH8 – Human Filamin A Ig-like domains 20-21* truncation (2141-2329)

Human Filamin A Ig-like domains 20-21*
MWexperimental 30 kDa
MWexpected 20 kDa
VPorod 32 nm3
log I(s) 2.99×101 2.99×100 2.99×10-1 2.99×10-2
Human Filamin A Ig-like domains 20-21* small angle scattering data  s, nm-1
ln I(s)
Human Filamin A Ig-like domains 20-21* Guinier plot ln 2.99×101 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Human Filamin A Ig-like domains 20-21* Kratky plot 1.104 0 √3 sRg
p(r)
Human Filamin A Ig-like domains 20-21* pair distance distribution function Rg: 2.0 nm 0 Dmax: 6.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Human Filamin A Ig-like domains 20-21* DAMMIF model
Synchrotron SAXS data from solutions of Human Filamin A Ig-like domains 20-21* truncation (2141-2329) in 20 mM Tris 50 mM NaCl 10mM DTT, pH 8 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.4 m and at a wavelength of λ = 0.93 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 mg/ml were measured . 10 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Filamin A fragment residues 2141-2329 (Ig-like domains).

Human Filamin A Ig-like domains 20-21* (FilaminA*)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   20 kDa
 
UniProt   P21333 (2141-2329)
Sequence   FASTA