Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties.

Pinotsis N, Chatziefthimiou SD, Berkemeier F, Beuron F, Mavridis IM, Konarev PV, Svergun DI, Morris E, Rief M, Wilmanns M, PLoS Biol 10(2):e1001261 (2012) Europe PMC

SASDLV5 – Myosin Filament-Linking Protein Myomesin-1 (domains My9-My13, dimer)

Myomesin-1
MWI(0) 125 kDa
MWexpected 121 kDa
log I(s) 3.58×106 3.58×105 3.58×104 3.58×103
Myomesin-1 small angle scattering data  s, nm-1
ln I(s)
Myomesin-1 Guinier plot ln 3.59×106 Rg: 9.6 nm 0 (9.6 nm)-2 s2
(sRg)2I(s)/I(0)
Myomesin-1 Kratky plot 1.104 0 √3 sRg
p(r)
Myomesin-1 pair distance distribution function Rg: 9.8 nm 0 Dmax: 37 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Myomesin-1 DAMMIN model
Synchrotron SAXS data from solutions of Myomesin-1 (domains My9-My13, dimer) in 25 mM Tris-HCl, 150 mM NaCl, pH 7.5 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 15.00 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Number of frames = UNKNOWN

Tags: X33
Myomesin-1 (MYOM1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   60.6 kDa
 
UniProt   P52179 (1152-1685)
Sequence   FASTA