Browse by MODEL: Ab initio only

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

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

SASDBQ4 – Neisseria meningitidis iron-regulated FrpD-FrpC lipoprotein/protein complex

Iron-regulated outer membrane lipoprotein FrpDIron-regulated protein FrpC experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Iron-regulated protein FrpC monomer, 46 kDa Neisseria meningitidis protein
Buffer: 50 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Oct 19
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep 7:40408 (2017)
Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 123 nm3

SASDB95 – Shigella outer membrane protein IcsA autotransporter

Outer membrane protein IcsA (53-758) experimental SAS data
DAMMIN model
Sample: Outer membrane protein IcsA (53-758) monomer, 72 kDa Shigella flexneri protein
Buffer: 50 mM Tris 150 mM NaCl 10 mM CaCl2 3% v/v glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 May 18
The Shigella Virulence Factor IcsA Relieves N-WASP Autoinhibition by Displacing the Verprolin Homology/Cofilin/Acidic (VCA) Domain. J Biol Chem 292(1):134-145 (2017)
Mauricio RP, Jeffries CM, Svergun DI, Deane JE
RgGuinier 3.7 nm
Dmax 13.2 nm
VolumePorod 103 nm3

SASDBW4 – Albumen gland precursor of ovorubin (lipoglycocarotenoprotein agPcOvo: an oligomeric protein)

Perivitellin ovorubin-1Perivitellin ovorubin-2Perivitellin ovorubin-3 experimental SAS data
DAMMIF model
Sample: Perivitellin ovorubin-1, 22 kDa Pomacea canaliculata protein
Perivitellin ovorubin-2, 24 kDa Pomacea canaliculata protein
Perivitellin ovorubin-3, 35 kDa Pomacea canaliculata protein
Buffer: 20 mM Tris-HCl, pH: 8.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2014 Jun 10
Apple Snail Perivitellin Precursor Properties Help Explain Predators' Feeding Behavior. Physiol Biochem Zool 90(4):461-470 (2017)
Cadierno MP, Dreon MS, Heras H
RgGuinier 4.3 nm
Dmax 14.9 nm
VolumePorod 526 nm3

SASDBX4 – Albumen gland precursor of perivitellin-2 (PcPV2)

Perivitellin-2 31 kDa subunitPerivitellin-2 67 kDa subunit experimental SAS data
DAMMIF model
Sample: Perivitellin-2 31 kDa subunit tetramer, 126 kDa Pomacea canaliculata protein
Perivitellin-2 67 kDa subunit tetramer, 250 kDa Pomacea canaliculata protein
Buffer: 20 mM Tris-HCl, pH: 8.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2014 Jun 10
Apple Snail Perivitellin Precursor Properties Help Explain Predators' Feeding Behavior. Physiol Biochem Zool 90(4):461-470 (2017)
Cadierno MP, Dreon MS, Heras H
RgGuinier 4.8 nm
Dmax 17.0 nm
VolumePorod 294 nm3

SASDBY6 – Leishmania braziliensis Mitochondrial heat shock protein 70 (LbmtHSP70)

Mitochondrial heat shock protein 70 experimental SAS data
DAMMIN model
Sample: Mitochondrial heat shock protein 70 monomer, 71 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 50 mM NacL, 5 mM KCl, 5 mM sodium phosphate, 2 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22
Structural and functional studies of the Leishmania braziliensis mitochondrial Hsp70: Similarities and dissimilarities to human orthologues. Arch Biochem Biophys 613:43-52 (2017)
Dores-Silva PR, Nishimura LS, Kiraly VT, Borges JC
RgGuinier 3.6 nm
Dmax 14.0 nm
VolumePorod 118 nm3