A study of the ultrastructure of fragile-X-related proteins.

Sjekloća L, Konarev PV, Eccleston J, Taylor IA, Svergun DI, Pastore A, Biochem J 419(2):347-57 (2009) Europe PMC

SASDMC7 – Nuclear fragile X mental retardation-interacting protein 2 (FRMP)

Nuclear fragile X mental retardation-interacting protein 2
MWexperimental 61 kDa
MWexpected 59 kDa
VPorod 92 nm3
log I(s) 2.70×102 2.70×101 2.70×100 2.70×10-1
Nuclear fragile X mental retardation-interacting protein 2 small angle scattering data  s, nm-1
ln I(s)
Nuclear fragile X mental retardation-interacting protein 2 Guinier plot ln 2.71×102 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
Nuclear fragile X mental retardation-interacting protein 2 Kratky plot 1.104 0 √3 sRg
p(r)
Nuclear fragile X mental retardation-interacting protein 2 pair distance distribution function Rg: 4.2 nm 0 Dmax: 15 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Nuclear fragile X mental retardation-interacting protein 2 DAMMIN model
Synchrotron SAXS data from solutions of Nuclear fragile X mental retardation-interacting protein 2 (FRMP) in 50 mM Tris-HCl pH 8.0, 5 mM TCEP 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). Solute concentrations ranging between 2 and 6 mg/ml were measured at 25°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.

Tags: X33
Nuclear fragile X mental retardation-interacting protein 2
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   59.1 kDa
 
UniProt   Q7Z417 (1-540)
Sequence   FASTA