Browse by ORGANISM: Homo sapiens (Human)

SASDVC2 – Human Haemoglobin (Sigma-Aldrich) with 5% PEG2000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml

Hemoglobin subunit betaHemoglobin subunit alphaProtoporphyrin IX containing fe experimental SAS data
Hemoglobin subunit beta Hemoglobin subunit alpha Protoporphyrin IX containing fe Kratky plot
Sample: Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Protoporphyrin IX containing fe monomer, 1 kDa
Buffer: 100mM Sodium Phosphate buffer with 5% (w/v) PEG2000, pH: 7
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Oct 6
Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications The Journal of Physical Chemistry B (2024)
Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B
RgGuinier 2.4 nm
Dmax 6.5 nm
VolumePorod 92 nm3

SASDVD2 – Human Haemoglobin (Sigma-Aldrich) with 5% (w/v) PEG4000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml

Hemoglobin subunit alphaHemoglobin subunit betaProtoporphyrin IX containing fe experimental SAS data
Hemoglobin subunit alpha Hemoglobin subunit beta Protoporphyrin IX containing fe Kratky plot
Sample: Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Protoporphyrin IX containing fe monomer, 1 kDa
Buffer: 100mM Sodium Phosphate buffer with 5% (w/v) PEG4000, pH: 7
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Oct 6
Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications The Journal of Physical Chemistry B (2024)
Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B
RgGuinier 2.4 nm
Dmax 6.1 nm
VolumePorod 91 nm3

SASDVE2 – Human Haemoglobin (Sigma-Aldrich) with 10% PEG2000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml

Hemoglobin subunit alphaHemoglobin subunit betaProtoporphyrin IX containing fe experimental SAS data
DAMMIF model
Sample: Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Protoporphyrin IX containing fe monomer, 1 kDa
Buffer: 100mM Sodium Phosphate buffer with 10% (w/v) PEG2000, pH: 7
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Oct 6
Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications The Journal of Physical Chemistry B (2024)
Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B
RgGuinier 2.8 nm
Dmax 11.3 nm
VolumePorod 131 nm3

SASDR52 – Human GluN1-GluN2A NMDA receptor at pH 8.0

Glutamate receptor ionotropic, NMDA 1Glutamate receptor ionotropic, NMDA 2A experimental SAS data
Glutamate receptor ionotropic, NMDA 1 Glutamate receptor ionotropic, NMDA 2A Kratky plot
Sample: Glutamate receptor ionotropic, NMDA 1 dimer, 193 kDa Homo sapiens protein
Glutamate receptor ionotropic, NMDA 2A dimer, 191 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 0.1% digitonin, 5 µM Cholesteryl Hemisuccinate TRIS Salt, 0.1 mM CHAPSO, 50 µM EDTA,1 mM Gly/Glu, 20 mM HEPES, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
Wang H, Xie C, Deng B, Ding J, Li N, Kou Z, Jin M, He J, Wang Q, Wen H, Zhang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 6.6 nm
Dmax 20.4 nm
VolumePorod 1180 nm3

SASDR62 – Human GluN1-GluN2A NMDA receptor in complex with human derived autoantibody mAb2G7 at pH 8.0

Glutamate receptor ionotropic, NMDA 1Glutamate receptor ionotropic, NMDA 2AHuman derived autoantibody mAb2G7 heavy chain, mAb2G7 VHHuman derived autoantibody mAb2G7 light chain, mAb2G7 VL experimental SAS data
Glutamate receptor ionotropic, NMDA 1 Glutamate receptor ionotropic, NMDA 2A Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH Human derived autoantibody mAb2G7 light chain, mAb2G7 VL Kratky plot
Sample: Glutamate receptor ionotropic, NMDA 1 dimer, 193 kDa Homo sapiens protein
Glutamate receptor ionotropic, NMDA 2A dimer, 191 kDa Homo sapiens protein
Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH dimer, 103 kDa protein
Human derived autoantibody mAb2G7 light chain, mAb2G7 VL dimer, 51 kDa protein
Buffer: 150 mM NaCl, 0.1% digitonin, 5 µM Cholesteryl Hemisuccinate TRIS Salt, 0.1 mM CHAPSO, 50 µM EDTA,1 mM Gly/Glu, 20 mM HEPES, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
Wang H, Xie C, Deng B, Ding J, Li N, Kou Z, Jin M, He J, Wang Q, Wen H, Zhang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 7.7 nm
Dmax 25.4 nm
VolumePorod 1260 nm3

SASDR72 – Human GluN1-GluN2A NMDA receptor in complex with human derived autoantibody mAb5F6 at pH 8.0

Glutamate receptor ionotropic, NMDA 1Glutamate receptor ionotropic, NMDA 2AHuman derived autoantibody mAb5F6 heavy chain, mAb5F6 VHHuman derived autoantibody mAb5F6 light chain, mAb5F6 VL experimental SAS data
Glutamate receptor ionotropic, NMDA 1 Glutamate receptor ionotropic, NMDA 2A Human derived autoantibody mAb5F6 heavy chain, mAb5F6 VH Human derived autoantibody mAb5F6 light chain, mAb5F6 VL Kratky plot
Sample: Glutamate receptor ionotropic, NMDA 1 dimer, 193 kDa Homo sapiens protein
Glutamate receptor ionotropic, NMDA 2A dimer, 191 kDa Homo sapiens protein
Human derived autoantibody mAb5F6 heavy chain, mAb5F6 VH dimer, 104 kDa Homo sapiens protein
Human derived autoantibody mAb5F6 light chain, mAb5F6 VL dimer, 52 kDa protein
Buffer: 150 mM NaCl, 0.1% digitonin, 5 µM Cholesteryl Hemisuccinate TRIS Salt, 0.1 mM CHAPSO, 50 µM EDTA,1 mM Gly/Glu, 20 mM HEPES, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
Wang H, Xie C, Deng B, Ding J, Li N, Kou Z, Jin M, He J, Wang Q, Wen H, Zhang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 9.9 nm
Dmax 31.7 nm
VolumePorod 2500 nm3

SASDVL5 – Small EDRK-rich factor 1 (SERF1a)

Isoform Short of Small EDRK-rich factor 1 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Mar 11
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.4 nm
Dmax 8.0 nm
VolumePorod 9 nm3

SASDVR5 – Small EDRK-rich factor 1 (SERF1a) bound to NT17 peptide

Isoform Short of Small EDRK-rich factor 1NT17 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
NT17 dimer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Oct 21
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm

SASDVS5 – Small EDRK-rich factor 1 (SERF1a) bound to HTT-3 peptide

Isoform Short of Small EDRK-rich factor 1HTT3 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
HTT3 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 May 20
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm
Dmax 7.2 nm
VolumePorod 9 nm3

SASDVZ5 – Human DNA repair protein RAD52 homolog (amino acids 1-212)

DNA repair protein RAD52 homolog experimental SAS data
DAMMIF model
Sample: DNA repair protein RAD52 homolog decamer, 234 kDa Homo sapiens protein
Buffer: 20 mM Bis-Tris, 10% glycerol, 400 mM NaCl, 100 mM KCl, 1 mM EDTA, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS 1000, Eppley Structural Biology Facility, University of Nebraska Medical Center on 2014 Jul 25
A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52 Journal of Structural Biology 216(3):108115 (2024)
Struble L, Lovelace J, Borgstahl G
RgGuinier 4.1 nm
Dmax 11.8 nm
VolumePorod 375 nm3