Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin.

Pinotsis N, Lange S, Perriard JC, Svergun DI, Wilmanns M, EMBO J 27(1):253-64 (2008) Europe PMC

SASDAK5 – Myomesin-1 My12-My13

Myomesin-1
MWI(0) 47 kDa
MWexpected 46 kDa
VPorod 56 nm3
log I(s) 1.00×104 1.00×103 1.00×102 1.00×101
Myomesin-1 small angle scattering data  s, nm-1
ln I(s)
Myomesin-1 Guinier plot ln 1.01×104 Rg: 4 nm 0 (4 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: 4.1 nm 0 Dmax: 14.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Myomesin-1 CRYSOL model
log I(s)
 s, nm-1
Myomesin-1 CRYSOL model
log I(s)
 s, nm-1
Myomesin-1 CRYSOL model
Synchrotron SAXS data from solutions of Myomesin-1 My12-My13 in 25 mM Tris/HCl 150 mM NaCl, pH 7.5 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 2.8 and 7.1 mg/ml were measured . 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.

Use of SAXS to discriminate between different crystallographic dimers of the C-terminal construct of myomesin-1 containing two IG-like domains.

Tags: X33
Myomesin-1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   22.9 kDa
 
UniProt   P52179 (1225-1443)
Sequence   FASTA