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

SASDAM4 – CRM1 Snu1

Exportin-1
Snurportin-1
MWexperimental 160 kDa
MWexpected 164 kDa
log I(s) 1.13×102 1.13×101 1.13×100 1.13×10-1
Exportin-1 Snurportin-1 small angle scattering data  s, nm-1
ln I(s)
Exportin-1 Snurportin-1 Guinier plot ln 1.13×102 Rg: 4.3 nm 0 (4.3 nm)-2 s2
(sRg)2I(s)/I(0)
Exportin-1 Snurportin-1 Kratky plot 1.104 0 √3 sRg
Dmax: 15 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Exportin-1 Snurportin-1 DAMMIF model
Synchrotron SAXS data from solutions of CRM1 Snu1 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 Pilatus 1M-W 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 1 and 10 mg/ml were measured at 10°C. Eight successive 15 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.

Storage temperature = UNKNOWN

Tags: X33
Exportin-1
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   123.1 kDa
 
UniProt   Q6P5F9
Sequence   FASTA
 
Snurportin-1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   41.1 kDa
 
UniProt   O95149
Sequence   FASTA