Browse by MODEL: Hybrid

SASDMQ7 – HOLO-serotransferrin at pH 5.5 in the presence of iron

Serotransferrin experimental SAS data
GASBOR model
Sample: Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer: 15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl, (APO Buffer), pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin International Journal of Molecular Sciences 22(24):13392 (2021)
Campos-Escamilla C, Siliqi D, Gonzalez-Ramirez L, Lopez-Sanchez C, Gavira J, Moreno A
RgGuinier 3.3 nm
Dmax 14.6 nm
VolumePorod 107 nm3

SASDMR7 – HOLO-serotransferrin at pH 7.0 in the presence of iron

Serotransferrin experimental SAS data
GASBOR model
Sample: Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer: 15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl (APO Buffer), pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin International Journal of Molecular Sciences 22(24):13392 (2021)
Campos-Escamilla C, Siliqi D, Gonzalez-Ramirez L, Lopez-Sanchez C, Gavira J, Moreno A
RgGuinier 3.2 nm
Dmax 13.5 nm
VolumePorod 103 nm3

SASDMS7 – HOLO-serotransferrin at pH 8.0 in the presence of iron

Serotransferrin experimental SAS data
GASBOR model
Sample: Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer: 15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl (Buffer APO-Tf-1), pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin International Journal of Molecular Sciences 22(24):13392 (2021)
Campos-Escamilla C, Siliqi D, Gonzalez-Ramirez L, Lopez-Sanchez C, Gavira J, Moreno A
RgGuinier 3.2 nm
Dmax 13.1 nm
VolumePorod 106 nm3

SASDKV7 – CCP2-SP domains of the complement C1r subcomponent

Complement C1r subcomponent experimental SAS data
PYMOL model
Sample: Complement C1r subcomponent monomer, 38 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 24
A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes. J Immunol 207(11):2856-2867 (2021)
Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL
RgGuinier 2.4 nm
Dmax 7.9 nm
VolumePorod 63 nm3

SASDKW7 – Complement inhibitory domain of the Borrelia burgdorferi fibronectin-binding protein BBK32

Fibronectin-binding protein BBK32 experimental SAS data
PYMOL model
Sample: Fibronectin-binding protein BBK32 monomer, 17 kDa Borreliella burgdorferi B31 protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 24
A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes. J Immunol 207(11):2856-2867 (2021)
Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 34 nm3

SASDKX7 – CCP2-SP domains of the complement C1r subcomponent bound to the complement inhibitory domain of the Borrelia burgdorferi fibronectin-binding protein BBK32

Fibronectin-binding protein BBK32Complement C1r subcomponent experimental SAS data
PYMOL model
Sample: Fibronectin-binding protein BBK32 monomer, 17 kDa Borrelia burgdorferi (strain … protein
Complement C1r subcomponent monomer, 38 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 24
A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes. J Immunol 207(11):2856-2867 (2021)
Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL
RgGuinier 2.8 nm
Dmax 8.6 nm
VolumePorod 75 nm3

SASDLT2 – 6D11 IgG monoclonal antibody

Anti-prion protein monoclonal IgG2a 6D11 experimental SAS data
CORAL model
Sample: Anti-prion protein monoclonal IgG2a 6D11 monomer, 145 kDa Mus musculus protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 15
Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies. Sci Adv 7(48):eabj1826 (2021)
Linsenmeier L, Mohammadi B, Shafiq M, Frontzek K, Bär J, Shrivastava AN, Damme M, Song F, Schwarz A, Da Vela S, Massignan T, Jung S, Correia A, Schmitz M, Puig B, Hornemann S, Zerr I, Tatzelt J, Biasini E, Saftig P, Schweizer M, Svergun D, Amin L, Mazzola F, Varani L, Thapa S, Gilch S, Schätzl H, Harris DA, Triller A, Mikhaylova M, Aguzzi A, Altmeppen HC, Glatzel M
RgGuinier 5.1 nm
Dmax 17.4 nm
VolumePorod 330 nm3

SASDLU2 – 2:1 complex between anti prion protein monoclonal IgG 6D11 and recombinant murine prion protein

Major prion proteinAnti-prion protein monoclonal IgG2a 6D11 experimental SAS data
OTHER model
Sample: Major prion protein monomer, 23 kDa Mus musculus protein
Anti-prion protein monoclonal IgG2a 6D11 monomer, 145 kDa Mus musculus protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 15
Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies. Sci Adv 7(48):eabj1826 (2021)
Linsenmeier L, Mohammadi B, Shafiq M, Frontzek K, Bär J, Shrivastava AN, Damme M, Song F, Schwarz A, Da Vela S, Massignan T, Jung S, Correia A, Schmitz M, Puig B, Hornemann S, Zerr I, Tatzelt J, Biasini E, Saftig P, Schweizer M, Svergun D, Amin L, Mazzola F, Varani L, Thapa S, Gilch S, Schätzl H, Harris DA, Triller A, Mikhaylova M, Aguzzi A, Altmeppen HC, Glatzel M
RgGuinier 8.1 nm
Dmax 24.8 nm
VolumePorod 710 nm3

SASDEX9 – Class II pyruvate aldolase (HpcH/HpaI aldolase), wild-type hexamer in HEPES isolated using SEC-SAXS

HpcH/HpaI aldolase experimental SAS data
GASBOR model
Sample: HpcH/HpaI aldolase hexamer, 165 kDa Rhizorhabdus wittichii RW1 protein
Buffer: 20 mM HEPES,, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 23
EFAMIX , a tool to decompose inline chromatography SAXS data from partially overlapping components Protein Science (2021)
Konarev P, Graewert M, Jeffries C, Fukuda M, Cheremnykh T, Volkov V, Svergun D
RgGuinier 3.3 nm
Dmax 9.4 nm
VolumePorod 233 nm3

SASDMP2 – Mouse Kirrel3 ectodomain

Kin of IRRE-like protein 3 experimental SAS data
SASREF model
Sample: Kin of IRRE-like protein 3 dimer, 106 kDa Mus musculus protein
Buffer: 10 mM HEPES pH 7.2, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 3
Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors. Cell Rep 37(5):109940 (2021)
Wang J, Vaddadi N, Pak JS, Park Y, Quilez S, Roman CA, Dumontier E, Thornton JW, Cloutier JF, Özkan E
RgGuinier 9.3 nm
Dmax 34.5 nm