Browse by ORGANISM: Homo sapiens (Human)

SASDAJ7 – Metal-free hETHE1, 1 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 8.3 nm
Dmax 38.0 nm
VolumePorod 602 nm3

SASDAK7 – Metal-free hETHE1, 2 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 8.8 nm
Dmax 42.5 nm
VolumePorod 647 nm3

SASDAL7 – Metal-free hETHE1, 3 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 11.2 nm
Dmax 56.0 nm
VolumePorod 1445 nm3

SASDAM7 – Metal-free hETHE1, 5 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 12.4 nm
Dmax 59.0 nm
VolumePorod 1820 nm3

SASDAN7 – Metal-free hETHE1, 10 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 14.2 nm
Dmax 63.5 nm
VolumePorod 2317 nm3

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

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)

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)

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

SASDB86 – apo-BRD4

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 12
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
Waring MJ, Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti P, Robb GR, Robers MB, Saif S, Stratton N, Svergun DI, Wang W, Whittaker D, Wilson DM, Yao Y
RgGuinier 7.0 nm
Dmax 27.0 nm

SASDB96 – Compound 1:BRD4 (1:1)

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 12
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
Waring MJ, Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti P, Robb GR, Robers MB, Saif S, Stratton N, Svergun DI, Wang W, Whittaker D, Wilson DM, Yao Y
RgGuinier 6.2 nm
Dmax 27.5 nm