SASBDB entries for UniProt ID:

SASDQZ9 – Beclin-1 amino acids 1-150 with two cysteine motifs, along with a C-terminal tyrosine analysed using EFA in BIOXTAS RAW software, component 0

UniProt ID: Q14457 (1-150) Beclin-1

Beclin-1 experimental SAS data
Beclin-1 Kratky plot
Sample: Beclin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 12
Invariant BECN1 CXXC motifs bind Zn(2+) and regulate structure and function of the BECN1 intrinsically disordered region. Autophagy :1-17 (2023)
Mukhopadhyay S, Subedi S, Hopkins JB, Ugrinov A, Chakravarthy S, Colbert CL, Sinha SC
RgGuinier 4.3 nm
Dmax 20.0 nm
VolumePorod 87 nm3

SASDR22 – Beclin-1 amino acids 1-150 with two cysteine motifs, along with a C-terminal tyrosine analysed using EFA in BIOXTAS RAW software, component 1

UniProt ID: Q14457 (1-150) Beclin-1

Beclin-1 experimental SAS data
Beclin-1 amino acids 1-150 with two cysteine motifs, along with a C-terminal tyrosine analysed using EFA in BIOXTAS RAW software, component 1 Rg histogram
Sample: Beclin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 12
Invariant BECN1 CXXC motifs bind Zn(2+) and regulate structure and function of the BECN1 intrinsically disordered region. Autophagy :1-17 (2023)
Mukhopadhyay S, Subedi S, Hopkins JB, Ugrinov A, Chakravarthy S, Colbert CL, Sinha SC
RgGuinier 2.8 nm
Dmax 12.0 nm
VolumePorod 49 nm3

SASDR52 – Human GluN1-GluN2A NMDA receptor at pH 8.0

UniProt ID: Q05586 (1-847) Glutamate receptor ionotropic, NMDA 1

UniProt ID: Q12879 (1-842) Glutamate receptor ionotropic, NMDA 2A

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

UniProt ID: Q05586 (1-847) Glutamate receptor ionotropic, NMDA 1

UniProt ID: Q12879 (1-842) Glutamate receptor ionotropic, NMDA 2A

UniProt ID: None (None-None) Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH

UniProt ID: None (None-None) Human derived autoantibody mAb2G7 light chain, mAb2G7 VL

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

UniProt ID: Q05586 (1-847) Glutamate receptor ionotropic, NMDA 1

UniProt ID: Q12879 (1-842) Glutamate receptor ionotropic, NMDA 2A

UniProt ID: None (None-None) Human derived autoantibody mAb5F6 heavy chain, mAb5F6 VH

UniProt ID: None (None-None) Human derived autoantibody mAb5F6 light chain, mAb5F6 VL

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

SASDRG2 – Ligand free Xenosiderophore Utilization System B (XusB)

UniProt ID: Q8A622 (41-464) DUF4374 domain-containing protein

DUF4374 domain-containing protein experimental SAS data
Sample: DUF4374 domain-containing protein monomer, 46 kDa Bacteroides thetaiotaomicron (strain … protein
Buffer: 20 mM Tris 150 mM NaCl, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 May 9
Iron acquisition by a commensal bacterium modifies host nutritional immunity during Salmonella infection. Cell Host Microbe 31(10):1639-1654.e10 (2023)
Spiga L, Fansler RT, Perera YR, Shealy NG, Munneke MJ, David HE, Torres TP, Lemoff A, Ran X, Richardson KL, Pudlo N, Martens EC, Folta-Stogniew E, Yang ZJ, Skaar EP, Byndloss MX, Chazin WJ, Zhu W
RgGuinier 2.3 nm
Dmax 7.4 nm
VolumePorod 74 nm3

SASDRH2 – Ligand bound Xenosiderophore Utilization System B (XusB)

UniProt ID: Q8A622 (41-464) DUF4374 domain-containing protein

DUF4374 domain-containing protein experimental SAS data
Sample: DUF4374 domain-containing protein monomer, 46 kDa Bacteroides thetaiotaomicron (strain … protein
Buffer: 20 mM Tris 150 mM NaCl, pH: 8
Experiment: SAXS data collected at 12-ID-B, Advanced Photon Source (APS), Argonne National Laboratory on 2021 May 9
Iron acquisition by a commensal bacterium modifies host nutritional immunity during Salmonella infection. Cell Host Microbe 31(10):1639-1654.e10 (2023)
Spiga L, Fansler RT, Perera YR, Shealy NG, Munneke MJ, David HE, Torres TP, Lemoff A, Ran X, Richardson KL, Pudlo N, Martens EC, Folta-Stogniew E, Yang ZJ, Skaar EP, Byndloss MX, Chazin WJ, Zhu W
RgGuinier 2.4 nm
Dmax 7.4 nm
VolumePorod 77 nm3

SASDRJ2 – Chicken Netrin-1 ΔC monomer (experiment ID: sm22113-7/sample1)

UniProt ID: Q90922 (26-458) Netrin-1

Netrin-1 experimental SAS data
Sample: Netrin-1 monomer, 50 kDa Gallus gallus protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Oct 24
The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation Nature Communications 14(1) (2023)
Meier M, Gupta M, Akgül S, McDougall M, Imhof T, Nikodemus D, Reuten R, Moya-Torres A, To V, Ferens F, Heide F, Padilla-Meier G, Kukura P, Huang W, Gerisch B, Mörgelin M, Poole K, Antebi A, Koch M, Stetefeld J
RgGuinier 4.0 nm
Dmax 18.0 nm
VolumePorod 103 nm3

SASDRK2 – Chicken Netrin-1 ΔC dimer (experiment ID: sm22113-7/sample1)

UniProt ID: Q90922 (26-458) Netrin-1

Netrin-1 experimental SAS data
Sample: Netrin-1 dimer, 99 kDa Gallus gallus protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Oct 24
The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation Nature Communications 14(1) (2023)
Meier M, Gupta M, Akgül S, McDougall M, Imhof T, Nikodemus D, Reuten R, Moya-Torres A, To V, Ferens F, Heide F, Padilla-Meier G, Kukura P, Huang W, Gerisch B, Mörgelin M, Poole K, Antebi A, Koch M, Stetefeld J
RgGuinier 5.9 nm
Dmax 21.3 nm
VolumePorod 145 nm3

SASDRL2 – Chicken Netrin-1 ΔC monomer (experiment ID: sm22113-7/sample11)

UniProt ID: Q90922 (26-458) Netrin-1

Netrin-1 experimental SAS data
Sample: Netrin-1 monomer, 50 kDa Gallus gallus protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Oct 24
The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation Nature Communications 14(1) (2023)
Meier M, Gupta M, Akgül S, McDougall M, Imhof T, Nikodemus D, Reuten R, Moya-Torres A, To V, Ferens F, Heide F, Padilla-Meier G, Kukura P, Huang W, Gerisch B, Mörgelin M, Poole K, Antebi A, Koch M, Stetefeld J
RgGuinier 4.1 nm
Dmax 21.0 nm
VolumePorod 84 nm3