SASBDB entries for UniProt ID:

SASDC53 – Colicin N Translocation domain

UniProt ID: P08083 (1-90) Colicin N Translocation domain

Colicin N Translocation domain experimental SAS data
Colicin N Translocation domain Rg histogram
Sample: Colicin N Translocation domain monomer, 10 kDa Escherichia coli protein
Buffer: 50 mM Na-Phosphate 300 mM NaCl, pH: 7.6
Experiment: SAXS data collected at BM29, ESRF on 2012 Jun 29
The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N. Biophys J 113(8):1673-1684 (2017)
Johnson CL, Solovyova AS, Hecht O, Macdonald C, Waller H, Grossmann JG, Moore GR, Lakey JH
RgGuinier 2.8 nm
Dmax 11.4 nm
VolumePorod 22 nm3

SASDC63 – Fowlpox Virus FPV039 antiapoptotic Bcl-2 viral protein in complex with BaK BH3 peptide (FPV039:BAK)

UniProt ID: Q9J5G4 (1-143) Bcl-2-like protein FPV039

UniProt ID: Q5F404 (72-97) Uncharacterized protein (BAK1)

Bcl-2-like protein FPV039Uncharacterized protein (BAK1) experimental SAS data
Bcl-2-like protein FPV039 Uncharacterized protein (BAK1) Kratky plot
Sample: Bcl-2-like protein FPV039 monomer, 17 kDa Fowlpox virus protein
Uncharacterized protein (BAK1) monomer, 3 kDa Gallus gallus protein
Buffer: 20 mM trisodium citrate pH, 200 mM NaCl, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Oct 2
Structural basis of apoptosis inhibition by the fowlpox virus protein FPV039. J Biol Chem 292(22):9010-9021 (2017)
Anasir MI, Caria S, Skinner MA, Kvansakul M
RgGuinier 2.0 nm

SASDC73 – Atg1-Atg13-Atg17-Atg31-Atg29 Minipentamer Complex

UniProt ID: Q6CSX2 (562-831) Serine/threonine-protein kinase ATG1

UniProt ID: Q6CWK2 (400-475) Autophagy-related protein 13

UniProt ID: Q6CS99 (1-423) Autophagy-related protein 17

UniProt ID: Q6CTU8 (1-85) Autophagy-related protein 29

UniProt ID: Q6CX74 (1-143) KLLA0A10637p

Serine/threonine-protein kinase ATG1Autophagy-related protein 13Autophagy-related protein 17Autophagy-related protein 29KLLA0A10637p experimental SAS data
Serine/threonine-protein kinase ATG1 Autophagy-related protein 13 Autophagy-related protein 17 Autophagy-related protein 29 KLLA0A10637p Kratky plot
Sample: Serine/threonine-protein kinase ATG1 dimer, 61 kDa Kluyveromyces lactis protein
Autophagy-related protein 13 dimer, 17 kDa Kluyveromyces lactis protein
Autophagy-related protein 17 dimer, 100 kDa Kluyveromyces lactis protein
Autophagy-related protein 29 dimer, 20 kDa Kluyveromyces lactis protein
KLLA0A10637p dimer, 32 kDa Kluyveromyces lactis protein
Buffer: 20 mM Tris, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Dec 20
Solution structure of the Atg1 complex: implications for the architecture of the phagophore assembly site. Structure 23(5):809-818 (2015)
Köfinger J, Ragusa MJ, Lee IH, Hummer G, Hurley JH
RgGuinier 10.3 nm
Dmax 34.0 nm
VolumePorod 1000 nm3

SASDC83 – Dimeric apoptosis regulator BAX (Bcl-2 associated X)

UniProt ID: Q07812 (1-192) Apoptosis regulator BAX (Bcl-2 associated X)

Apoptosis regulator BAX (Bcl-2 associated X) experimental SAS data
CORAL model
Sample: Apoptosis regulator BAX (Bcl-2 associated X) dimer, 42 kDa Homo sapiens protein
Buffer: 20mM sodium phosphate 100mM NaCl, pH: 8
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2015 May 28
Oligomerization process of Bcl-2 associated X protein revealed from intermediate structures in solution. Phys Chem Chem Phys 19(11):7947-7954 (2017)
Shih O, Yeh YQ, Liao KF, Sung TC, Chiang YW, Jeng US
RgGuinier 3.0 nm
Dmax 9.5 nm
VolumePorod 86 nm3

SASDC93 – Tetrameric apoptosis regulator BAX (Bcl-2 associated X)

UniProt ID: Q07812 (1-192) Apoptosis regulator BAX (Bcl-2 associated X)

Apoptosis regulator BAX (Bcl-2 associated X) experimental SAS data
SASREF model
Sample: Apoptosis regulator BAX (Bcl-2 associated X) tetramer, 85 kDa Homo sapiens protein
Buffer: 20mM sodium phosphate 100mM NaCl, pH: 8
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2015 May 28
Oligomerization process of Bcl-2 associated X protein revealed from intermediate structures in solution. Phys Chem Chem Phys 19(11):7947-7954 (2017)
Shih O, Yeh YQ, Liao KF, Sung TC, Chiang YW, Jeng US
RgGuinier 3.6 nm
Dmax 12.0 nm
VolumePorod 180 nm3

SASDCA3 – Zinc finger and BTB domain-containing protein 38 (ZBTB38) complexed with methylated C-terminal ZBTB38 binding sequence

UniProt ID: Q8NAP3 (1006-1152) Zinc finger and BTB domain-containing protein 38

UniProt ID: (None-None) methylated C-terminal ZBTB38 binding sequence

Zinc finger and BTB domain-containing protein 38methylated C-terminal ZBTB38 binding sequence experimental SAS data
MONSA model
Sample: Zinc finger and BTB domain-containing protein 38 monomer, 17 kDa Homo sapiens protein
Methylated C-terminal ZBTB38 binding sequence monomer, 17 kDa DNA
Buffer: 10 mM Tris, 1 mM tris(2-carboxy-ethyl)phosphine (TCEP), 0.05% NaN3, 10% D2O, pH: 6.8
Experiment: SAXS data collected at Anton Paar SAXSess, Department of Chemistry, University of Utah on 2016 Nov 11
The C-Terminal Zinc Fingers of ZBTB38 are Novel Selective Readers of DNA Methylation. J Mol Biol 430(3):258-271 (2018)
Pozner A, Hudson NO, Trewhella J, Terooatea TW, Miller SA, Buck-Koehntop BA
RgGuinier 2.5 nm
Dmax 8.2 nm
VolumePorod 50 nm3

SASDCC3 – Nucleolysin TIA-1 isoform p40 in complex with U15 RNA

UniProt ID: P31483-2 (None-None) Nucleolysin TIA-1 isoform p40

UniProt ID: (None-None) poly U 15mer

Nucleolysin TIA-1 isoform p40poly U 15mer experimental SAS data
Nucleolysin TIA-1 isoform p40 poly U 15mer Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 30 kDa Homo sapiens protein
Poly U 15mer monomer, 5 kDa RNA
Buffer: 10 mM Potassium Phosphate 50 mM NaCl 10 mM DTT, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2016 Apr 28
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins. Angew Chem Int Ed Engl 56(32):9322-9325 (2017)
Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
RgGuinier 2.4 nm
Dmax 8.7 nm
VolumePorod 39 nm3

SASDCD3 – Nucleolysin TIA-1 isoform p40 (LPQTG containing construct for sortase mediated protein ligation)

UniProt ID: P31483-2 (None-None) Nucleolysin TIA-1 isoform p40

Nucleolysin TIA-1 isoform p40 experimental SAS data
Nucleolysin TIA-1 isoform p40 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 31 kDa Homo sapiens protein
Buffer: 10 mM Potassium Phosphate 50 mM NaCl 10 mM DTT, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2015 Dec 1
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins. Angew Chem Int Ed Engl 56(32):9322-9325 (2017)
Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
RgGuinier 2.7 nm
Dmax 10.3 nm
VolumePorod 38 nm3

SASDCE3 – Nucleolysin TIA-1 isoform p40 in complex with U15 RNA (LPQTG containing construct for sortase mediated protein ligation)

UniProt ID: (None-None) poly U 15mer

UniProt ID: P31483-2 (None-None) Nucleolysin TIA-1 isoform p40

poly U 15merNucleolysin TIA-1 isoform p40 experimental SAS data
poly U 15mer Nucleolysin TIA-1 isoform p40 Kratky plot
Sample: Poly U 15mer monomer, 5 kDa RNA
Nucleolysin TIA-1 isoform p40 monomer, 31 kDa Homo sapiens protein
Buffer: 10 mM Potassium Phosphate 50 mM NaCl 10 mM DTT, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2015 Dec 1
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins. Angew Chem Int Ed Engl 56(32):9322-9325 (2017)
Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
RgGuinier 2.4 nm
Dmax 8.6 nm
VolumePorod 40 nm3

SASDCF3 – Nucleolysin TIA-1 isoform p40

UniProt ID: P31483-2 (None-None) Nucleolysin TIA-1 isoform p40

Nucleolysin TIA-1 isoform p40 experimental SAS data
Nucleolysin TIA-1 isoform p40 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 30 kDa Homo sapiens protein
Buffer: 10 mM Potassium Phosphate 50 mM NaCl 10 mM DTT, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2016 Apr 28
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins. Angew Chem Int Ed Engl 56(32):9322-9325 (2017)
Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
RgGuinier 2.7 nm
Dmax 11.2 nm
VolumePorod 38 nm3