SASBDB entries for UniProt ID:

SASDBU7 – DNA binding domain (DBD) of chromo domain-containing protein 1 (Chd1: 1009-1274)

UniProt ID: P32657 (1009-1274) chromodomain helicase DNA binding domain
chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 31 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 20
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 2.6 nm
Dmax 8.3 nm

SASDBV7 – Chromo-ATPase-DBD domains of chromo domain-containing protein 1 (Chd1: 133-1305)

UniProt ID: P32657 (133-1305) chromodomain helicase DNA binding domain
chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 135 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2008 Nov 30
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 4.2 nm
Dmax 15.4 nm
VolumePorod 280 nm3

SASDBW7 – N-terminal and chromo-ATPase-DBD domains of chromo domain-containing protein 1 (Chd1: 1-1305)

UniProt ID: P32657 (1-1305) chromodomain helicase DNA binding domain
chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 150 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 30
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 4.9 nm
Dmax 16.0 nm
VolumePorod 340 nm3

SASDBX7 – Chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010)

UniProt ID: P32657 (133-1010) chromodomain helicase DNA binding domain
chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 102 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 30
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 4.1 nm
Dmax 16.1 nm
VolumePorod 190 nm3

SASDBY7 – N-terminal and chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010)

UniProt ID: P32657 (1-1010) chromodomain helicase DNA binding domain
chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 117 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 30
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 4.5 nm
Dmax 12.0 nm
VolumePorod 228 nm3

SASDBZ7 – Complement factor 1s in complex with Complement factor 1r

UniProt ID: P00736 (18-705) Complement C1r subcomponent

UniProt ID: P09871 (16-688) Complement C1s subcomponent
Complement C1r subcomponentComplement C1s subcomponent experimental SAS data
CORAL model
Sample: Complement C1r subcomponent dimer, 156 kDa Homo sapiens protein
Complement C1s subcomponent dimer, 150 kDa Homo sapiens protein
Buffer: 50 mM TrisHCl, 145 mM NaCl, 3 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 8
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade. Proc Natl Acad Sci U S A 114(5):986-991 (2017)
Mortensen SA, Sander B, Jensen RK, Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR
RgGuinier 11.6 nm

SASDB28 – Complement factor 1q (C1q)

UniProt ID: P02747 (23-245) Complement C1q subcomponent subunit C

UniProt ID: P02746 (28-253) Complement C1q subcomponent subunit B

UniProt ID: P02745 (23-245) Complement C1q subcomponent subunit A
Complement C1q subcomponent subunit CComplement C1q subcomponent subunit BComplement C1q subcomponent subunit A experimental SAS data
Complement C1q subcomponent subunit C Complement C1q subcomponent subunit B Complement C1q subcomponent subunit A Kratky plot
Sample: Complement C1q subcomponent subunit C hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit B hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit A hexamer, 142 kDa Homo sapiens protein
Buffer: 50 mM TrisHCl, 145 mM NaCl, 3 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 8
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade. Proc Natl Acad Sci U S A 114(5):986-991 (2017)
Mortensen SA, Sander B, Jensen RK, Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR
RgGuinier 12.6 nm

SASDB38 – Inactivated complement factor 1 (C1)

UniProt ID: P02747 (23-245) Complement C1q subcomponent subunit C

UniProt ID: P02746 (28-253) Complement C1q subcomponent subunit B

UniProt ID: P02745 (23-245) Complement C1q subcomponent subunit A

UniProt ID: P00736 (18-705) Complement C1r subcomponent

UniProt ID: P09871 (16-688) Complement C1s subcomponent
Complement C1q subcomponent subunit CComplement C1q subcomponent subunit BComplement C1q subcomponent subunit AComplement C1r subcomponentComplement C1s subcomponent experimental SAS data
CORAL model
Sample: Complement C1q subcomponent subunit C hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit B hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit A hexamer, 142 kDa Homo sapiens protein
Complement C1r subcomponent dimer, 156 kDa Homo sapiens protein
Complement C1s subcomponent dimer, 150 kDa Homo sapiens protein
Buffer: 50 mM EPPS, 145 mM NaCl, 3 mM CaCl2, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Aug 16
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade. Proc Natl Acad Sci U S A 114(5):986-991 (2017)
Mortensen SA, Sander B, Jensen RK, Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR
RgGuinier 11.5 nm
Dmax 36.6 nm

SASDB78 – Probable ATP-dependent RNA helicase DDX58 (Full-length RIG-I)

UniProt ID: O95786 (1-925) Probable ATP-dependent RNA helicase DDX58
Probable ATP-dependent RNA helicase DDX58 experimental SAS data
BUNCH model
Sample: Probable ATP-dependent RNA helicase DDX58 monomer, 108 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 2.5 mM MgCl2, 10% glycerol and 1mM DTT, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Apr 6
Combined roles of ATP and small hairpin RNA in the activation of RIG-I revealed by solution-based analysis. Nucleic Acids Res 46(6):3169-3186 (2018)
Shah N, Beckham SA, Wilce JA, Wilce MCJ
RgGuinier 4.3 nm
Dmax 14.0 nm
VolumePorod 186 nm3

SASDB88 – Probable ATP-dependent RNA helicase DDX58 (Full-length RIG-I) plus ADP-AlFx

UniProt ID: O95786 (1-925) Probable ATP-dependent RNA helicase DDX58
Probable ATP-dependent RNA helicase DDX58 experimental SAS data
EOM/RANCH model
Sample: Probable ATP-dependent RNA helicase DDX58 monomer, 108 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 2.5 mM MgCl2, 10% glycerol and 1mM DTT, 2mM ADP-AlFx, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Nov 20
Combined roles of ATP and small hairpin RNA in the activation of RIG-I revealed by solution-based analysis. Nucleic Acids Res 46(6):3169-3186 (2018)
Shah N, Beckham SA, Wilce JA, Wilce MCJ
RgGuinier 4.2 nm
Dmax 15.6 nm
VolumePorod 190 nm3