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 Aug 6)
PMID: 23850451
doi: 10.1016/j.str.2013.05.015
Published in SASBDB:

SASDAJ4 – CRM1

Exportin-1 experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3
RgGuinier 3.8 nm
Dmax 11.0 nm
VolumePorod 190 nm3

SASDAK4 – CRM1 RanGTP

Exportin-1GTP-binding nuclear protein Ran experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3
RgGuinier 3.6 nm
Dmax 10.0 nm

SASDAL4 – CRM1 RanGTP Snu1

Exportin-1GTP-binding nuclear protein RanSnurportin-1 experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein
Snurportin-1 monomer, 41 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3
RgGuinier 4.1 nm
Dmax 14.0 nm

SASDAM4 – CRM1 Snu1

Exportin-1Snurportin-1 experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
Snurportin-1 monomer, 41 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 10
RgGuinier 4.3 nm
Dmax 15.0 nm