SASBDB entries for UniProt ID:

SASDXX3 – Transthyretin tetramer with over-saturated tolcapone

UniProt ID: P02766 (21-147) Transthyretin

UniProt ID: None (None-None) Tolcapone
TransthyretinTolcapone experimental SAS data
COOT model
Sample: Transthyretin tetramer, 55 kDa Homo sapiens protein
Tolcapone dimer, 1 kDa
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 19
Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR. J Appl Crystallogr 58(Pt 4):1373-1383 (2025)
Shih O, Feng YC, Agrawal S, Liao KF, Yeh YQ, Chang JW, Yu TY, Jeng US
RgGuinier 2.5 nm
Dmax 8.6 nm
VolumePorod 107 nm3

SASDXY3 – Transthyretin tetramer with over-saturated tafamidis

UniProt ID: P02766 (21-147) Transthyretin

UniProt ID: None (None-None) Tafamidis
TransthyretinTafamidis experimental SAS data
COOT model
Sample: Transthyretin tetramer, 55 kDa Homo sapiens protein
Tafamidis dimer, 1 kDa
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 19
Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR. J Appl Crystallogr 58(Pt 4):1373-1383 (2025)
Shih O, Feng YC, Agrawal S, Liao KF, Yeh YQ, Chang JW, Yu TY, Jeng US
RgGuinier 2.5 nm
Dmax 9.0 nm
VolumePorod 69 nm3

SASDX84 – Peroxisomal targeting signal receptor Pex5 from P. pastoris

UniProt ID: P33292 (1-576) Peroxisomal targeting signal receptor
Peroxisomal targeting signal receptor experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Peroxisomal targeting signal receptor monomer, 65 kDa Komagataella pastoris protein
Buffer: 50 mM HEPES, 150 mM NaCl, 3% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 May 15
Structure of Pex8 in complex with peroxisomal receptor Pex5 reveals its essential role in peroxisomal cargo translocation (2025)
Ekal L, Wendscheck D, David Y, Chojnowski G, Jeffries C, Mullapudi E, Schuldiner M, Warscheid B, Zalckvar E, Wilmanns M
RgGuinier 5.0 nm
Dmax 21.4 nm
VolumePorod 131 nm3

SASDX94 – Peroxisomal biogenesis factor 8 (Pex8) from P. pastoris

UniProt ID: Q01962 (33-713) Peroxisomal biogenesis factor 8
Peroxisomal biogenesis factor 8 experimental SAS data
MULTIFOXS model
Sample: Peroxisomal biogenesis factor 8 monomer, 78 kDa Komagataella pastoris protein
Buffer: 50 mM HEPES, 150 mM NaCl, 3% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Aug 17
Structure of Pex8 in complex with peroxisomal receptor Pex5 reveals its essential role in peroxisomal cargo translocation (2025)
Ekal L, Wendscheck D, David Y, Chojnowski G, Jeffries C, Mullapudi E, Schuldiner M, Warscheid B, Zalckvar E, Wilmanns M
RgGuinier 3.6 nm
Dmax 13.0 nm
VolumePorod 117 nm3

SASDXA4 – Peroxisomal biogenesis factor 8 (Pex8) bound to Peroxisomal targeting signal receptor, Pex5 from P. pastoris

UniProt ID: P33292 (1-576) Peroxisomal targeting signal receptor

UniProt ID: Q01962 (33-713) Peroxisomal biogenesis factor 8
Peroxisomal targeting signal receptorPeroxisomal biogenesis factor 8 experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Peroxisomal targeting signal receptor monomer, 65 kDa Komagataella pastoris protein
Peroxisomal biogenesis factor 8 monomer, 78 kDa Komagataella pastoris protein
Buffer: 50 mM HEPES, 150 mM NaCl, 3% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Aug 17
Structure of Pex8 in complex with peroxisomal receptor Pex5 reveals its essential role in peroxisomal cargo translocation (2025)
Ekal L, Wendscheck D, David Y, Chojnowski G, Jeffries C, Mullapudi E, Schuldiner M, Warscheid B, Zalckvar E, Wilmanns M
RgGuinier 5.1 nm
Dmax 23.5 nm
VolumePorod 247 nm3

SASDXB4 – Peroxisomal biogenesis factor 8 (Pex8) bound to the N-terminal domain of Peroxisomal targeting signal receptor, Pex5 (Pex8-Pex5NTD complex from P. pastoris)

UniProt ID: Q01962 (33-713) Peroxisomal biogenesis factor 8

UniProt ID: P33292 (1-276) Peroxisomal targeting signal receptor
Peroxisomal biogenesis factor 8Peroxisomal targeting signal receptor experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Peroxisomal biogenesis factor 8 monomer, 78 kDa Komagataella pastoris protein
Peroxisomal targeting signal receptor monomer, 32 kDa Komagataella pastoris protein
Buffer: 50 mM HEPES, 150 mM NaCl, 3% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Aug 17
Structure of Pex8 in complex with peroxisomal receptor Pex5 reveals its essential role in peroxisomal cargo translocation (2025)
Ekal L, Wendscheck D, David Y, Chojnowski G, Jeffries C, Mullapudi E, Schuldiner M, Warscheid B, Zalckvar E, Wilmanns M
RgGuinier 4.6 nm
Dmax 19.0 nm
VolumePorod 177 nm3

SASDXC4 – Peroxisomal biogenesis factor 8 (Pex8) bound to the C-terminal domain of Peroxisomal targeting signal receptor, Pex5 (Pex8-Pex5CTD complex from P. pastoris)

UniProt ID: Q01962 (33-713) Peroxisomal biogenesis factor 8

UniProt ID: P33292 (259-576) Peroxisomal targeting signal receptor
Peroxisomal biogenesis factor 8Peroxisomal targeting signal receptor experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Peroxisomal biogenesis factor 8 monomer, 78 kDa Komagataella pastoris protein
Peroxisomal targeting signal receptor monomer, 36 kDa Komagataella pastoris protein
Buffer: 50 mM HEPES, 150 mM NaCl, 3% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Aug 17
Structure of Pex8 in complex with peroxisomal receptor Pex5 reveals its essential role in peroxisomal cargo translocation (2025)
Ekal L, Wendscheck D, David Y, Chojnowski G, Jeffries C, Mullapudi E, Schuldiner M, Warscheid B, Zalckvar E, Wilmanns M
RgGuinier 4.2 nm
Dmax 14.5 nm
VolumePorod 141 nm3

SASDXD4 – Full-length human SFPQ dimer (protiated and deuterated)

UniProt ID: P23246 (214-707) Splicing factor, proline- and glutamine-rich
Splicing factor, proline- and glutamine-rich experimental SAS data
Splicing factor, proline- and glutamine-rich Kratky plot
Sample: Splicing factor, proline- and glutamine-rich dimer, 153 kDa Homo sapiens protein
Buffer: 150 mM KCl, 1.5% glycerol, 20 mM HEPES, 1 mM DTT (in 100% H2O), pH: 7.4
Experiment: SANS data collected at Quokka - Small Angle Neutron Scattering, Australian Centre for Neutron Scattering (ANSTO) on 2023 Jan 23
Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation Acta Crystallographica Section D Structural Biology 81(7):357-379 (2025)
Koning H, Lai V, Sethi A, Chakraborty S, Ang C, Fox A, Duff A, Whitten A, Marshall A, Bond C
RgGuinier 8.7 nm
Dmax 30.7 nm
VolumePorod 241000 nm3

SASDX45 – IgA protease (ThomasA) 31-1167

UniProt ID: Q9AES2 (31-1167) IgA protease
IgA protease experimental SAS data
IgA protease Kratky plot
Sample: IgA protease monomer, 127 kDa Thomasclavelia ramosa protein
Buffer: 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 2% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Apr 19
Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases The EMBO Journal (2025)
Márquez-Moñino M, Martínez Gascueña A, Azzam T, Persson A, Manzanares-Gomez A, Aguillo-Urarte M, Brown T, Montero-Sagarminaga A, Lood R, Naegeli A, Connell S, Sastre D, Sundberg E, Trastoy B
RgGuinier 6.4 nm
Dmax 25.0 nm
VolumePorod 208 nm3

SASDX55 – IgA protease (ThomasA) 31-878

UniProt ID: Q9AES2 (31-878) IgA protease
IgA protease experimental SAS data
IgA protease Kratky plot
Sample: IgA protease monomer, 96 kDa Thomasclavelia ramosa protein
Buffer: 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 2% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Apr 19
Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases The EMBO Journal (2025)
Márquez-Moñino M, Martínez Gascueña A, Azzam T, Persson A, Manzanares-Gomez A, Aguillo-Urarte M, Brown T, Montero-Sagarminaga A, Lood R, Naegeli A, Connell S, Sastre D, Sundberg E, Trastoy B
RgGuinier 3.4 nm
Dmax 10.6 nm
VolumePorod 101 nm3