SASBDB entries for UniProt ID:

SASDRW6 – YdaS, a cro-type repressor from Escherichai coli O157:H7 cryptic prophage CP-933

UniProt ID: Q8XAD7 (1-100) Phage antirepressor protein Cro
Phage antirepressor protein Cro experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Phage antirepressor protein Cro monomer, 12 kDa Escherichia coli O157:H7 protein
Buffer: 20 mM sodium acetate, 150 mM NaCl, 1 mM TCEP, pH: 5.5
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Feb 5
Structural-function relationship of YdaS, a Cro-type repressor in the cryptic prophage CP-933P from Escherichia coli O157:H7
Marusa Prolic Kalinsek
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 19 nm3

SASDRX6 – lantibiotic dehydratase MadB (apo)

UniProt ID: K6TUQ9 (1-1038) Thiopeptide-type bacteriocin biosynthesis domain containing protein
Thiopeptide-type bacteriocin biosynthesis domain containing protein experimental SAS data
GASBOR model
Sample: Thiopeptide-type bacteriocin biosynthesis domain containing protein dimer, 250 kDa Clostridium sp. Maddingley … protein
Buffer: 50 mM HEPES, 200 mM NaCl, 1 % (v/v) Glycerol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 26
Structural insights into the substrate binding mechanism of the class I dehydratase MadB Communications Biology 8(1) (2025)
Knospe C, Ortiz J, Reiners J, Kedrov A, Gertzen C, Smits S, Schmitt L
RgGuinier 4.5 nm
Dmax 13.6 nm
VolumePorod 440 nm3

SASDRY6 – lantibiotic dehydratase MadB bound to truncated maddinglicin with a full leader peptide (Leader3)

UniProt ID: K6TUQ9 (1-1038) Thiopeptide-type bacteriocin biosynthesis domain containing protein

UniProt ID: K6SWQ2 (1-33) Lantibiotic, gallidermin/nisin family
Thiopeptide-type bacteriocin biosynthesis domain containing proteinLantibiotic, gallidermin/nisin family experimental SAS data
GASBOR model
Sample: Thiopeptide-type bacteriocin biosynthesis domain containing protein dimer, 250 kDa Clostridium sp. Maddingley … protein
Lantibiotic, gallidermin/nisin family monomer, 3 kDa Clostridium sp. Maddingley … protein
Buffer: 50 mM HEPES, 200 mM NaCl, 1 % (v/v) Glycerol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2020 Dec 3
Structural insights into the substrate binding mechanism of the class I dehydratase MadB Communications Biology 8(1) (2025)
Knospe C, Ortiz J, Reiners J, Kedrov A, Gertzen C, Smits S, Schmitt L
RgGuinier 4.5 nm
Dmax 13.8 nm
VolumePorod 445 nm3

SASDRZ6 – D1-D2 N-terminal domains of thrombospondin type-1 domain-containing protein 7A

UniProt ID: Q9UPZ6 (48-192) Thrombospondin type-1 domain-containing protein 7A
Thrombospondin type-1 domain-containing protein 7A experimental SAS data
ALPHAFOLD PROTEIN STRUCTURE DATABASE model
Sample: Thrombospondin type-1 domain-containing protein 7A monomer, 17 kDa Homo sapiens protein
Buffer: 25mM Tris, 150 mM NaCl, 5 mM NaNO3, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Aug 23
Structure of the N-terminal didomain d1_d2 of the Thrombospondin type-1 domain-containing 7A (2023)
Bochel A, Mortensen S, Seifert L, Hengel F, Jeffries C, Chojnowski G, Kretz O, Huber T, Tomas N, Wilmanns M
RgGuinier 2.5 nm
Dmax 9.5 nm
VolumePorod 28 nm3

SASDR27 – Triple mutant (D116A, H118A, Y176A) of the D1-D2 N-terminal domains of thrombospondin type-1 domain-containing protein 7A

UniProt ID: Q9UPZ6 (48-192) Thrombospondin type-1 domain-containing protein 7A (D116A, H118A, Y176A)
Thrombospondin type-1 domain-containing protein 7A (D116A, H118A, Y176A) experimental SAS data
Triple mutant (D116A, H118A, Y176A) of the D1-D2 N-terminal domains of thrombospondin type-1 domain-containing protein 7A Rg histogram
Sample: Thrombospondin type-1 domain-containing protein 7A (D116A, H118A, Y176A) monomer, 16 kDa Homo sapiens protein
Buffer: 25mM Tris, 150 mM NaCl, 5 mM NaNO3, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Dec 2
Structure of the N-terminal didomain d1_d2 of the Thrombospondin type-1 domain-containing 7A (2023)
Bochel A, Mortensen S, Seifert L, Hengel F, Jeffries C, Chojnowski G, Kretz O, Huber T, Tomas N, Wilmanns M
RgGuinier 2.7 nm
Dmax 11.5 nm
VolumePorod 19 nm3

SASDR37 – HOTag6 tetramerization domain followed by a Gly-Ser linker fused to human monoubiquitin

UniProt ID: None (1-76) HOTag-GS-Ubiquitin
HOTag-GS-Ubiquitin experimental SAS data
HOTag-GS-Ubiquitin Kratky plot
Sample: HOTag-GS-Ubiquitin tetramer, 51 kDa synthetic construct protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 16
Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units Proceedings of the National Academy of Sciences 120(42) (2023)
Galagedera S, Dao T, Enos S, Chaudhuri A, Schmit J, Castañeda C
RgGuinier 3.7 nm
Dmax 14.0 nm
VolumePorod 74 nm3

SASDR47 – HOTag6 tetramerization domain followed by a (Gly-Ser)2 linker fused to human monoubiquitin

UniProt ID: None (1-76) HOTag6-(GS)2-Ubiquitin
HOTag6-(GS)2-Ubiquitin experimental SAS data
HOTag6-(GS)2-Ubiquitin Kratky plot
Sample: HOTag6-(GS)2-Ubiquitin tetramer, 52 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2023 Feb 21
Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units Proceedings of the National Academy of Sciences 120(42) (2023)
Galagedera S, Dao T, Enos S, Chaudhuri A, Schmit J, Castañeda C
RgGuinier 3.7 nm
Dmax 13.7 nm
VolumePorod 69 nm3

SASDR57 – HOTag6 tetramerization domain followed by a (Gly-Ser)4 linker fused to human monoubiquitin

UniProt ID: None (1-76) HOTag-(GS)4-Ubiquitin
HOTag-(GS)4-Ubiquitin experimental SAS data
HOTag-(GS)4-Ubiquitin Kratky plot
Sample: HOTag-(GS)4-Ubiquitin tetramer, 53 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 16
Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units Proceedings of the National Academy of Sciences 120(42) (2023)
Galagedera S, Dao T, Enos S, Chaudhuri A, Schmit J, Castañeda C
RgGuinier 3.8 nm
Dmax 14.3 nm
VolumePorod 76 nm3

SASDR67 – HOTag6 tetramerization domain followed by a (Gly-Ser)10 linker fused to human monoubiquitin

UniProt ID: None (1-76) HOTag-(GS)10-Ubiquitin
HOTag-(GS)10-Ubiquitin experimental SAS data
HOTag-(GS)10-Ubiquitin Kratky plot
Sample: HOTag-(GS)10-Ubiquitin tetramer, 56 kDa synthetic construct protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 16
Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units Proceedings of the National Academy of Sciences 120(42) (2023)
Galagedera S, Dao T, Enos S, Chaudhuri A, Schmit J, Castañeda C
RgGuinier 4.0 nm
Dmax 14.8 nm
VolumePorod 84 nm3

SASDR77 – HOTag6 tetramerization domain followed by a (Gly-Ser)25 linker fused to human monoubiquitin

UniProt ID: None (1-76) HOTag6-(GS)25-Ubiquitin
HOTag6-(GS)25-Ubiquitin experimental SAS data
HOTag6-(GS)25-Ubiquitin Kratky plot
Sample: HOTag6-(GS)25-Ubiquitin tetramer, 65 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2023 Feb 21
Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units Proceedings of the National Academy of Sciences 120(42) (2023)
Galagedera S, Dao T, Enos S, Chaudhuri A, Schmit J, Castañeda C
RgGuinier 4.7 nm
Dmax 19.3 nm
VolumePorod 117 nm3