SASBDB entries for UniProt ID:

SASDQT9 – Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with fourth BRC repeat (BRC4)

UniProt ID: Q06609 (1-339) DNA repair protein RAD51 homolog 1 (F86E A89E)

UniProt ID: P51587 (1517-1551) Breast cancer type 2 susceptibility protein
DNA repair protein RAD51 homolog 1 (F86E A89E)Breast cancer type 2 susceptibility protein experimental SAS data
Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with fourth BRC repeat (BRC4) Rg histogram
Sample: DNA repair protein RAD51 homolog 1 (F86E A89E) monomer, 37 kDa Homo sapiens protein
Breast cancer type 2 susceptibility protein monomer, 4 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 50 mM Na2SO4, 2% v/v sucrose, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Dec 7
Isolation and characterization of monomeric human RAD51: a novel tool for investigating homologous recombination in cancer Angewandte Chemie International Edition (2023)
Rinaldi F, Schipani F, Balboni B, Catalano F, Marotta R, Myers S, Previtali V, Veronesi M, Scietti L, Cecatiello V, Pasqualato S, Ortega J, Girotto S, Cavalli A
RgGuinier 2.9 nm
Dmax 15.6 nm
VolumePorod 70 nm3

SASDQU9 – His-Tagged Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with His-tagged fourth BRC repeat (BRC4)

UniProt ID: Q06609 (1-339) DNA repair protein RAD51 homolog 1 (F86E, A89E, His-Tagged)

UniProt ID: P51587 (1517-1551) Breast cancer type 2 susceptibility protein
DNA repair protein RAD51 homolog 1 (F86E, A89E, His-Tagged)Breast cancer type 2 susceptibility protein experimental SAS data
His-Tagged Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with His-tagged fourth BRC repeat (BRC4) Rg histogram
Sample: DNA repair protein RAD51 homolog 1 (F86E, A89E, His-Tagged) monomer, 40 kDa Homo sapiens protein
Breast cancer type 2 susceptibility protein monomer, 6 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 200 mM Na2SO4, 5% glycerol, 0.1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Apr 7
Isolation and characterization of monomeric human RAD51: a novel tool for investigating homologous recombination in cancer Angewandte Chemie International Edition (2023)
Rinaldi F, Schipani F, Balboni B, Catalano F, Marotta R, Myers S, Previtali V, Veronesi M, Scietti L, Cecatiello V, Pasqualato S, Ortega J, Girotto S, Cavalli A
RgGuinier 3.0 nm
Dmax 16.5 nm
VolumePorod 78 nm3

SASDQV9 – Nanobody1 in complex with the extracellular domain of human BCMA

UniProt ID: Q02223 (1-54) Tumor necrosis factor receptor superfamily member 17

UniProt ID: None (None-None) Nanobody1
Tumor necrosis factor receptor superfamily member 17Nanobody1 experimental SAS data
Tumor necrosis factor receptor superfamily member 17 Nanobody1 Kratky plot
Sample: Tumor necrosis factor receptor superfamily member 17 monomer, 6 kDa Homo sapiens protein
Nanobody1 monomer, 14 kDa protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2022 Aug 28
Antigen-induced chimeric antigen receptor multimerization amplifies on-tumor cytotoxicity. Signal Transduct Target Ther 8(1):445 (2023)
Sun Y, Yang XN, Yang SS, Lyu YZ, Zhang B, Liu KW, Li N, Cui JC, Huang GX, Liu CL, Xu J, Mi JQ, Chen Z, Fan XH, Chen SJ, Chen S
RgGuinier 3.0 nm
Dmax 9.8 nm
VolumePorod 52 nm3

SASDQW9 – Nanobody2 in complex with the extracellular domain of human BCMA

UniProt ID: Q02223 (1-54) Tumor necrosis factor receptor superfamily member 17

UniProt ID: None (None-None) Nanobody2
Tumor necrosis factor receptor superfamily member 17Nanobody2 experimental SAS data
Tumor necrosis factor receptor superfamily member 17 Nanobody2 Kratky plot
Sample: Tumor necrosis factor receptor superfamily member 17 monomer, 6 kDa Homo sapiens protein
Nanobody2 monomer, 14 kDa protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2022 Aug 28
Antigen-induced chimeric antigen receptor multimerization amplifies on-tumor cytotoxicity. Signal Transduct Target Ther 8(1):445 (2023)
Sun Y, Yang XN, Yang SS, Lyu YZ, Zhang B, Liu KW, Li N, Cui JC, Huang GX, Liu CL, Xu J, Mi JQ, Chen Z, Fan XH, Chen SJ, Chen S
RgGuinier 2.0 nm
Dmax 9.0 nm
VolumePorod 24 nm3

SASDQX9 – Tandem nanobody in complex with the extracellular domain of human BCMA

UniProt ID: Q02223 (1-54) Tumor necrosis factor receptor superfamily member 17

UniProt ID: None (None-None) Tandem nanobody
Tumor necrosis factor receptor superfamily member 17Tandem nanobody experimental SAS data
Tumor necrosis factor receptor superfamily member 17 Tandem nanobody Kratky plot
Sample: Tumor necrosis factor receptor superfamily member 17 monomer, 6 kDa Homo sapiens protein
Tandem nanobody monomer, 27 kDa protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2022 Aug 28
Antigen-induced chimeric antigen receptor multimerization amplifies on-tumor cytotoxicity. Signal Transduct Target Ther 8(1):445 (2023)
Sun Y, Yang XN, Yang SS, Lyu YZ, Zhang B, Liu KW, Li N, Cui JC, Huang GX, Liu CL, Xu J, Mi JQ, Chen Z, Fan XH, Chen SJ, Chen S
RgGuinier 5.1 nm
Dmax 23.3 nm
VolumePorod 247 nm3

SASDQY9 – Beclin-1 amino acids 1-150 with cysteine motif residues mutated to serine, along with a C-terminal tyrosine

UniProt ID: Q14457 (1-150) Beclin-1 (C18S, C21S, A103V, C137S, C140S)
Beclin-1 (C18S, C21S, A103V, C137S, C140S) experimental SAS data
Beclin-1 amino acids 1-150 with cysteine motif residues mutated to serine, along with a C-terminal tyrosine Rg histogram
Sample: Beclin-1 (C18S, C21S, A103V, C137S, C140S) 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 4.1 nm
Dmax 19.3 nm
VolumePorod 57 nm3

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