SASBDB entries for UniProt ID:

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

UniProt ID: P43351 (1-212) DNA repair protein RAD52 homolog
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

SASDV26 – Human DNA repair protein RAD52 homolog (amino acids 1-303)

UniProt ID: P43351 (1-303) DNA repair protein RAD52 homolog
DNA repair protein RAD52 homolog experimental SAS data
DAMMIF model
Sample: DNA repair protein RAD52 homolog nonamer, 300 kDa Homo sapiens protein
Buffer: 20 mM Bis-Tris, 10% GLycerol, 400 mM NaCl, 100 mM KCl, 1mM 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 4.8 nm
Dmax 18.3 nm
VolumePorod 782 nm3

SASDV46 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD

UniProt ID: P10636-8 (244-372) Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M
RgGuinier 3.5 nm
Dmax 12.2 nm
VolumePorod 33 nm3

SASDV56 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317

UniProt ID: P10636-8 (244-372) Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)

UniProt ID: A0A091E260 (1-77) Polyubiquitin-B
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317 Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M
RgGuinier 3.3 nm
Dmax 13.3 nm
VolumePorod 41 nm3

SASDV66 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C353

UniProt ID: P10636-8 (244-372) Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)

UniProt ID: A0A091E260 (1-77) Polyubiquitin-B
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C353 Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M
RgGuinier 3.1 nm
Dmax 12.1 nm
VolumePorod 33 nm3

SASDV76 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to two Ubiquitins at tau residues C311 and C317

UniProt ID: P10636-8 (244-372) Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)

UniProt ID: A0A091E260 (1-77) Polyubiquitin-B

UniProt ID: A0A091E260 (1-77) Polyubiquitin-B
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-BPolyubiquitin-B experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to two Ubiquitins at tau residues C311 and C317 Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M
RgGuinier 3.3 nm
Dmax 12.2 nm
VolumePorod 59 nm3

SASDVD6 – The Ig-like C2-type 4 domain (Ig4WT) of Palladin

UniProt ID: Q9ET54 (1154-1257) Palladin
Palladin experimental SAS data
SASREF model
Sample: Palladin monomer, 12 kDa Mus musculus protein
Buffer: 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl, pH:
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS. Protein Sci 34(5):e70122 (2025)
Sargent R, Liu DH, Yadav R, Glennenmeier D, Bradford C, Urbina N, Beck MR
RgGuinier 1.7 nm
Dmax 6.8 nm
VolumePorod 18 nm3

SASDVE6 – The Ig-like C2-type 3 domain (Ig3WT) of Palladin

UniProt ID: Q9ET54 (1022-1126) Palladin
Palladin experimental SAS data
SASREF model
Sample: Palladin monomer, 12 kDa Mus musculus protein
Buffer: 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl, pH:
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS. Protein Sci 34(5):e70122 (2025)
Sargent R, Liu DH, Yadav R, Glennenmeier D, Bradford C, Urbina N, Beck MR
RgGuinier 1.6 nm
Dmax 6.7 nm
VolumePorod 18 nm3

SASDVF6 – The Ig-like C2-type 3 and Ig-like C2-type 4 domains (Ig34WT) of Palladin

UniProt ID: Q9ET54 (1022-1257) Palladin
Palladin experimental SAS data
The Ig-like C2-type 3 and Ig-like C2-type 4 domains (Ig34WT) of Palladin Rg histogram
Sample: Palladin monomer, 27 kDa Mus musculus protein
Buffer: 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl, pH:
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS. Protein Sci 34(5):e70122 (2025)
Sargent R, Liu DH, Yadav R, Glennenmeier D, Bradford C, Urbina N, Beck MR
RgGuinier 2.8 nm
Dmax 12.3 nm
VolumePorod 29 nm3

SASDVG6 – 2-nitroimidazole nitrohydrolase

UniProt ID: F4ZCI3 (1-379) 2-nitroimidazole nitrohydrolase (T2I, G14D, K73R)
2-nitroimidazole nitrohydrolase (T2I, G14D, K73R) experimental SAS data
REFMAC model
Sample: 2-nitroimidazole nitrohydrolase (T2I, G14D, K73R) hexamer, 258 kDa Mycobacterium sp. (strain … protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5% (v/v) glycerol, pH: 7.6
Experiment: SAXS data collected at BioSAXS, Australian Synchrotron on 2024 Aug 6
Structural insights into the enzymatic breakdown of azomycin-derived antibiotics by 2-nitroimdazole hydrolase (NnhA). Commun Biol 7(1):1676 (2024)
Ahmed FH, Liu JW, Royan S, Warden AC, Esquirol L, Pandey G, Newman J, Scott C, Peat TS
RgGuinier 4.6 nm
Dmax 12.6 nm
VolumePorod 363 nm3