Structural determinants and mechanism of mammalian CRM1 allostery.

Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A, Structure 21(8):1350-60 (2013) Europe PMC

SASDAJ4 – CRM1

Exportin-1
MWexperimental 120 kDa
MWexpected 123 kDa
VPorod 190 nm3
log I(s) 1.15×100 1.15×10-1 1.15×10-2 1.15×10-3
Exportin-1 small angle scattering data  s, nm-1
ln I(s)
Exportin-1 Guinier plot ln 1.15×100 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Exportin-1 Kratky plot 1.104 0 3 sRg
Dmax: 11 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Exportin-1 DAMMIF model

Synchrotron SAXS data from solutions of CRM1 in 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, 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 1 and 10 mg/ml were measured at 10°C. One 120 second frame was 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.

Wavelength = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Tags: X33
Exportin-1
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   123.1 kDa
 
UniProt   Q6P5F9
Sequence   FASTA