SASBDB entries for UniProt ID:

SASDWN6 – RAD51 [F86E, A89E] in complex with BRCA2 truncation containing the first, second, third and fourth BRC repeats (BRC1-4) SEC-SAXS

UniProt ID: P51587 (1002-1551) Breast cancer type 2 susceptibility protein (BRC repeats 1-4)

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

Breast cancer type 2 susceptibility protein (BRC repeats 1-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
ALPHAFOLD model
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 1-4) monomer, 62 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) tetramer, 148 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 100 mM Li₂SO₄, 1 mM DTT, 1% sucrose, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 7.7 nm
Dmax 34.0 nm
VolumePorod 409 nm3

SASDWP6 – RAD51 [F86E, A89E] in complex with BRCA2 truncation containing the first, second, third and fourth BRC repeats (BRC1-4) at 0.5 mg/mL

UniProt ID: P51587 (1002-1551) Breast cancer type 2 susceptibility protein (BRC repeats 1-4)

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

Breast cancer type 2 susceptibility protein (BRC repeats 1-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 1-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 1-4) monomer, 62 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) tetramer, 148 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 8.1 nm
Dmax 33.0 nm
VolumePorod 422 nm3

SASDWQ6 – RAD51 [F86E, A89E] in complex with BRCA2 truncation containing the first, second, third and fourth BRC repeats (BRC1-4) at 0.98 mg/mL

UniProt ID: P51587 (1002-1551) Breast cancer type 2 susceptibility protein (BRC repeats 1-4)

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

Breast cancer type 2 susceptibility protein (BRC repeats 1-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 1-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 1-4) monomer, 62 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) tetramer, 148 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 7.6 nm
Dmax 33.3 nm
VolumePorod 392 nm3

SASDWR6 – RAD51 [F86E, A89E] in complex with BRCA2 truncation containing the first, second, third and fourth BRC repeats (BRC1-4) at 2 mg/mL

UniProt ID: P51587 (1002-1551) Breast cancer type 2 susceptibility protein (BRC repeats 1-4)

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

Breast cancer type 2 susceptibility protein (BRC repeats 1-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 1-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 1-4) monomer, 62 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) tetramer, 148 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 7.7 nm
Dmax 33.0 nm
VolumePorod 417 nm3

SASDWU6 – Human anterior gradient protein 2 (AGR2)

UniProt ID: O95994 (41-171) Anterior gradient protein 2 homolog

Anterior gradient protein 2 homolog experimental SAS data
MULTIFOXS model
Sample: Anterior gradient protein 2 homolog dimer, 30 kDa Homo sapiens protein
Buffer: 20 mM Tris pH7.4, 150 mM NaCl, 1% glycerol, 0.2 mM TCEP, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 May 5
A structural basis for chaperone repression of stress signaling from the endoplasmic reticulum. Mol Cell (2025)
Neidhardt L, Tung J, Kuchersky M, Milczarek J, Kargas V, Stott K, Rosenzweig R, Ron D, Yan Y
RgGuinier 2.0 nm
Dmax 6.3 nm
VolumePorod 30 nm3

SASDWV6 – SEC-SAXS data for the monomeric (24mer) fraction of horse spleen apoferritin

UniProt ID: P02791 (2-175) Ferritin light chain

Ferritin light chain experimental SAS data
CHIMERA model
Sample: Ferritin light chain 24-mer, 476 kDa Equus caballus protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, 0.9 mM CaCl2, 0.5 mM MgCl2, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 May 24
Structural insights into the nature of static and dynamic apoferritin dimers
Aleksei Tsarenko
RgGuinier 5.4 nm
Dmax 13.5 nm
VolumePorod 651 nm3

SASDWW6 – SEC-SAXS data for the total dimer (2 x 24mer) fraction of horse spleen apoferritin

UniProt ID: P02791 (2-175) Ferritin light chain

Ferritin light chain experimental SAS data
CHIMERA model
Sample: Ferritin light chain, 953 kDa Equus caballus protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, 0.9 mM CaCl2, 0.5 mM MgCl2, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 May 24
Structural insights into the nature of static and dynamic apoferritin dimers
Aleksei Tsarenko
RgGuinier 7.7 nm
Dmax 25.0 nm
VolumePorod 1751 nm3

SASDWX6 – SEC-SAXS data for presumably dynamic dimers (2 x 24mer) of horse spleen apoferritin

UniProt ID: P02791 (2-175) Ferritin light chain

Ferritin light chain experimental SAS data
CHIMERA model
Sample: Ferritin light chain, 953 kDa Equus caballus protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, 0.9 mM CaCl2, 0.5 mM MgCl2, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 May 24
Structural insights into the nature of static and dynamic apoferritin dimers
Aleksei Tsarenko
RgGuinier 8.0 nm
Dmax 26.8 nm
VolumePorod 1369 nm3

SASDWY6 – SEC-SAXS data for presumably disulfide-bounded dimers (2 x 24mer) of horse spleen apoferritin

UniProt ID: P02791 (2-175) Ferritin light chain

Ferritin light chain experimental SAS data
CHIMERA model
Sample: Ferritin light chain, 953 kDa Equus caballus protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, 0.9 mM CaCl2, 0.5 mM MgCl2, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 May 24
Structural insights into the nature of static and dynamic apoferritin dimers
Aleksei Tsarenko
RgGuinier 8.1 nm
Dmax 25.0 nm
VolumePorod 1677 nm3

SASDWZ6 – ABC transporter permease protein extracellular domain from S.agalactiae (SaNsrP ECD)

UniProt ID: Q8DZX0 (311-412) ABC transporter, permease protein, extracellular domain

ABC transporter, permease protein, extracellular domain experimental SAS data
ABC transporter, permease protein, extracellular domain Kratky plot
Sample: ABC transporter, permease protein, extracellular domain monomer, 23 kDa Streptococcus agalactiae serotype … protein
Buffer: 25 mM MES, 500 mM NaCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2020 Dec 3
The extracellular domain of SaNSrFP binds bacitracin and allows the identification of new members of the BceAB transporter family Frontiers in Microbiology 16 (2025)
Mammen C, Gottstein J, Cea P, Tantsur K, Reiners J, Bonus M, Gohlke H, Smits S
RgGuinier 2.4 nm
Dmax 9.0 nm
VolumePorod 50 nm3