SASBDB entries for UniProt ID:

SASDMQ6 – The N-terminus of E3 ubiquitin-protein ligase DTX3L (M1-Q200)

UniProt ID: Q8TDB6 (1-200) E3 ubiquitin-protein ligase DTX3L
E3 ubiquitin-protein ligase DTX3L experimental SAS data
E3 ubiquitin-protein ligase DTX3L Kratky plot
Sample: E3 ubiquitin-protein ligase DTX3L pentamer, 114 kDa Homo sapiens protein
Buffer: 30 mM HEPES, 350 mM NaCl, 10% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 6
Reconstitution of the DTX3L-PARP9 complex reveals determinants for high affinity heterodimerization and multimeric assembly. Biochem J (2022)
Ashok Y, Vela-Rodríguez C, Yang CS, Alanen HI, Liu F, Paschal BM, Lehtiö L
RgGuinier 4.7 nm
Dmax 17.0 nm
VolumePorod 200 nm3

SASDMS6 – Non-POU domain-containing octamer-binding protein (NONO homodimer)

UniProt ID: Q15233 (53-312) Non-POU domain-containing octamer-binding protein
Non-POU domain-containing octamer-binding protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-Cl (pH 7.5), 250 mM KCl, 50 mM L-proline, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28
Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1. Nucleic Acids Res (2021)
Knott GJ, Chong YS, Passon DM, Liang XH, Deplazes E, Conte MR, Marshall AC, Lee M, Fox AH, Bond CS
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 96 nm3

SASDMT6 – Non-POU domain-containing octamer-binding protein (NONO homodimer) bound to an antisense oligonucleotide

UniProt ID: Q15233 (53-312) Non-POU domain-containing octamer-binding protein

UniProt ID: None (None-None) 5-10-5 gapmer phosphorothioate antisense oligonucleotide tetramer
Non-POU domain-containing octamer-binding protein5-10-5 gapmer phosphorothioate antisense oligonucleotide tetramer experimental SAS data
SASREF model
Sample: Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein
5-10-5 gapmer phosphorothioate antisense oligonucleotide tetramer tetramer, 28 kDa
Buffer: 20 mM Tris-Cl (pH 7.5), 250 mM KCl, 50 mM L-proline, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28
Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1. Nucleic Acids Res (2021)
Knott GJ, Chong YS, Passon DM, Liang XH, Deplazes E, Conte MR, Marshall AC, Lee M, Fox AH, Bond CS
RgGuinier 3.9 nm
Dmax 18.4 nm
VolumePorod 153 nm3

SASDMY6 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length

UniProt ID: Q9HC16 (1-384) DNA dC->dU-editing enzyme APOBEC-3G
DNA dC->dU-editing enzyme APOBEC-3G experimental SAS data
DAMFILT model
Sample: DNA dC->dU-editing enzyme APOBEC-3G tetramer, 186 kDa Homo sapiens protein
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 4.2 nm
Dmax 13.3 nm
VolumePorod 350 nm3

SASDMZ6 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length in complex with DNA: tetramer

UniProt ID: Q9HC16 (1-384) DNA dC->dU-editing enzyme APOBEC-3G

UniProt ID: None (None-None) 40-mer single stranded inhibitory DNA
DNA dC->dU-editing enzyme APOBEC-3G40-mer single stranded inhibitory DNA experimental SAS data
DAMFILT model
Sample: DNA dC->dU-editing enzyme APOBEC-3G tetramer, 186 kDa Homo sapiens protein
40-mer single stranded inhibitory DNA dimer, 24 kDa DNA
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 4.7 nm
Dmax 16.2 nm
VolumePorod 395 nm3

SASDM27 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length in complex with DNA: monomer

UniProt ID: None (None-None) 40-mer single stranded inhibitory DNA

UniProt ID: Q9HC16 (1-384) DNA dC->dU-editing enzyme APOBEC-3G
40-mer single stranded inhibitory DNADNA dC->dU-editing enzyme APOBEC-3G experimental SAS data
DAMFILT model
Sample: 40-mer single stranded inhibitory DNA monomer, 12 kDa DNA
DNA dC->dU-editing enzyme APOBEC-3G monomer, 46 kDa Homo sapiens protein
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 3.1 nm
Dmax 10.0 nm
VolumePorod 118 nm3

SASDM67 – Hemolysin A (HlyA) from Escherichia coli UTI89

UniProt ID: P08715 (1-1024) Hemolysin, plasmid (Hemolysin A)
Hemolysin, plasmid (Hemolysin A) experimental SAS data
GASBOR model
Sample: Hemolysin, plasmid (Hemolysin A) dimer, 220 kDa Escherichia coli UTI89 protein
Buffer: 100 mM HEPES pH 8.0, 250 mM NaCl, 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Mar 6
Identity Determinants of the Translocation Signal for a Type 1 Secretion System Frontiers in Physiology 12 (2022)
Spitz O, Erenburg I, Kanonenberg K, Peherstorfer S, Lenders M, Reiners J, Ma M, Luisi B, Smits S, Schmitt L
RgGuinier 6.7 nm
Dmax 25.3 nm
VolumePorod 346 nm3

SASDM77 – Full-length polypyrimidine tract binding protein (PTB)

UniProt ID: Q9UKA9 (1-531) Polypyrimidine tract-binding protein 2
Polypyrimidine tract-binding protein 2 experimental SAS data
DAMMIN model
Sample: Polypyrimidine tract-binding protein 2 monomer, 57 kDa Homo sapiens protein
Buffer: 25 mM Tris, 250 mM NaCl, 2 mM DTT, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Feb 11
Structure and RNA interactions of the N-terminal RRM domains of PTB. Structure 12(9):1631-43 (2004)
Simpson PJ, Monie TP, Szendröi A, Davydova N, Tyzack JK, Conte MR, Read CM, Cary PD, Svergun DI, Konarev PV, Curry S, Matthews S
RgGuinier 4.0 nm
Dmax 14.0 nm
VolumePorod 117 nm3

SASDMA7 – Prion protein aggregate in solution

UniProt ID: P04156 (1-253) Major prion protein
Major prion protein experimental SAS data
DAMMIN model
Sample: Major prion protein 24-mer, 664 kDa Homo sapiens protein
Buffer: 5 mM sodium acetate, pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jun 2
Structural characterization of beta-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro. J Struct Biol 157(2):308-20 (2007)
Redecke L, von Bergen M, Clos J, Konarev PV, Svergun DI, Fittschen UE, Broekaert JA, Bruns O, Georgieva D, Mandelkow E, Genov N, Betzel C
RgGuinier 9.8 nm
Dmax 32.0 nm
VolumePorod 3320 nm3

SASDMB7 – Glucosamine-6-phosphate Synthase from Candida albicans

UniProt ID: Q59RW5 (1-493) N-acetylglucosamine kinase 1
N-acetylglucosamine kinase 1 experimental SAS data
DAMMIN model
Sample: N-acetylglucosamine kinase 1 tetramer, 219 kDa Candida albicans (strain … protein
Buffer: 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Apr 28
The crystal and solution studies of glucosamine-6-phosphate synthase from Candida albicans. J Mol Biol 372(3):672-88 (2007)
Raczynska J, Olchowy J, Konariev PV, Svergun DI, Milewski S, Rypniewski W
RgGuinier 5.1 nm
Dmax 16.0 nm
VolumePorod 421 nm3