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

SASDMN9 – Conformational characterization of A77-78 fibronectin type III tandem

Titin
MWexperimental 17 kDa
MWexpected 22 kDa
VPorod 21 nm3
log I(s) 9.82×101 9.82×100 9.82×10-1 9.82×10-2
Titin small angle scattering data  s, nm-1
ln I(s)
Titin Guinier plot ln 9.83×101 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Titin Kratky plot 1.104 0 √3 sRg
p(r)
Titin pair distance distribution function Rg: 25.6 nm 0 Dmax: 90 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Titin OTHER model
log I(s)
 s, nm-1
Titin DAMMIF model
Synchrotron SAXS data from solutions of Conformational characterization of A77-78 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 14.00 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 (A77-A78)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   21.7 kDa
 
UniProt   Q8WZ42
Sequence   FASTA