The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin

Bucher R, Svergun D, Muhle-Goll C, Mayans O, Journal of Molecular Biology 401(5):843-853 (2010) DOI

SASDMQ9 – Conformational characterization of A84-86 fibronectin type III tandem

Titin
MWexperimental 29 kDa
MWexpected 32 kDa
log I(s) 6.76×103 6.76×102 6.76×101 6.76×100
Titin small angle scattering data  s, nm-1
ln I(s)
Titin Guinier plot ln 6.77×103 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Titin Kratky plot 1.104 0 √3 sRg
p(r)
Titin pair distance distribution function 0 Dmax: 14 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Titin SASREF model
log I(s)
 s, nm-1
Titin DAMMIF model
Synchrotron SAXS data from solutions of Conformational characterization of A84-86 fibronectin type III tandem in 100 mM NaCl, 50 mM Tris-HCl, 2mM DTT, pH 7.2 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Tags: X33
Titin (A84-A86)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   31.5 kDa
 
UniProt   Q8WZ42
Sequence   FASTA