Browse by ORGANISM: Mus musculus (Mouse)

SASDAS7 – mouse olfactomedin-1

Noelin experimental SAS data
DAMMIF model
Sample: Noelin tetramer, 256 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 6
Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure. J Biol Chem 290(24):15092-101 (2015)
Pronker MF, Bos TG, Sharp TH, Thies-Weesie DM, Janssen BJ
RgGuinier 8.5 nm
Dmax 30.0 nm
VolumePorod 616 nm3

SASDAX5 – Endophilin-CoA complex

Endophilin-A1 BAR domainarachidonyl-CoA experimental SAS data
SASREF model
Sample: Endophilin-A1 BAR domain dimer, 58 kDa Mus musculus protein
Arachidonyl-CoA, 60 kDa
Buffer: 50 mM TRIS-HCL 300 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Nov 27
Endophilin-A1 BAR domain interaction with arachidonyl CoA. Front Mol Biosci 1:20 (2014)
Petoukhov MV, Weissenhorn W, Svergun DI
RgGuinier 5.9 nm
Dmax 19.0 nm
VolumePorod 480 nm3

SASDAY5 – Free endophilin

Endophilin-A1 BAR domain experimental SAS data
CORAL model
Sample: Endophilin-A1 BAR domain dimer, 58 kDa Mus musculus protein
Buffer: 50 mM TRIS-HCL 300 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Feb 13
Endophilin-A1 BAR domain interaction with arachidonyl CoA. Front Mol Biosci 1:20 (2014)
Petoukhov MV, Weissenhorn W, Svergun DI
RgGuinier 3.3 nm
Dmax 13.5 nm
VolumePorod 90 nm3

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
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
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
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
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
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
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
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
RgGuinier 4.3 nm
Dmax 15.0 nm

SASDH62 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 7
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 123 nm3

SASDH72 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 8
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 151 nm3

SASDH82 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 11
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.6 nm
Dmax 11.4 nm
VolumePorod 145 nm3