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

SASDAK4 – CRM1 RanGTP

Exportin-1
GTP-binding nuclear protein Ran
MWexperimental 140 kDa
MWexpected 148 kDa
log I(s) 1.65×100 1.65×10-1 1.65×10-2 1.65×10-3
Exportin-1 GTP-binding nuclear protein Ran small angle scattering data  s, nm-1
ln I(s)
Exportin-1 GTP-binding nuclear protein Ran Guinier plot ln 1.66×100 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Exportin-1 GTP-binding nuclear protein Ran Kratky plot 1.104 0 √3 sRg
Dmax: 10 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Exportin-1 GTP-binding nuclear protein Ran DAMMIF model
log I(s)
 s, nm-1
Exportin-1 GTP-binding nuclear protein Ran MONSA model
log I(s)
 s, nm-1
Exportin-1 GTP-binding nuclear protein Ran MONSA model
Synchrotron SAXS data from solutions of CRM1 RanGTP 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 2M 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.

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
 
GTP-binding nuclear protein Ran
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   24.4 kDa
 
UniProt   P62826
Sequence   FASTA