Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer.

Sjekloća L, Pudas R, Sjöblom B, Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylänne J, Djinović Carugo K, J Mol Biol 368(4):1011-23 (2007) Europe PMC

SASDAC4 – FilaminC 23-24

Filamin C 23-24
MWexperimental 42 kDa
MWexpected 40 kDa
VPorod 75 nm3
log I(s) 1.22×102 1.22×101 1.22×100 1.22×10-1
Filamin C 23-24 small angle scattering data  s, nm-1
ln I(s)
Filamin C 23-24 Guinier plot ln 1.22×102 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Filamin C 23-24 Kratky plot 1.104 0 √3 sRg
p(r)
Filamin C 23-24 pair distance distribution function Rg: 3.5 nm 0 Dmax: 13 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Filamin C 23-24 DAMMIN model
log I(s)
 s, nm-1
Filamin C 23-24 BUNCH model
Synchrotron SAXS data from solutions of FilaminC 23-24 in 20 mM Tris-HCl 50 mM NaCl, pH 8 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 5 and 21 mg/ml were measured at 10°C. Two successive 120 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.

Wavelength = UNKNOWN. Sample detector distance = UNKNOWN

Tags: X33
Filamin C 23-24 (FilaminC 23-24)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   20 kDa
Sequence   FASTA