Browse by MACROMOLECULE type: protein

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

SASDB65 – Tyrosine-protein phosphatase (YopH)/putative yopH targeting protein (SycH) heterotrimeric complex

SycH putative yopH targeting proteinTyrosine-protein phosphatase YopH experimental SAS data
CRYSOL model
Sample: SycH putative yopH targeting protein dimer, 32 kDa Yersinia pseudotuberculosis protein
Tyrosine-protein phosphatase YopH monomer, 14 kDa Yersinia pseudotuberculosis protein
Buffer: 50 mM HEPES 2mM TCEP, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Aug 1
Global Disordering in Stereo-Specific Protein Association Biophysical Journal 112(3):33a (2017)
Gupta A, Reinartz I, Spilotros A, Jonna V, Hofer A, Svergun D, Schug A, Wolf-Watz M
RgGuinier 3.0 nm
Dmax 12.5 nm
VolumePorod 89 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

SASDBP4 – Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD

Iron-regulated outer membrane lipoprotein FrpD experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Buffer: 10 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 2.2 nm
Dmax 6.5 nm
VolumePorod 41 nm3

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

SASDB47 – Full length tetrameric FKBP39 protein from Drosophila melanogaster

39 kDa FK506-binding nuclear protein experimental SAS data
Full length tetrameric FKBP39 protein from Drosophila melanogaster Rg histogram
Sample: 39 kDa FK506-binding nuclear protein tetramer, 163 kDa Drosophila melanogaster protein
Buffer: 50 mM Na2HPO4 150 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2014 Nov 14
Nucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments. Sci Rep 7:40405 (2017)
Kozłowska M, Tarczewska A, Jakób M, Bystranowska D, Taube M, Kozak M, Czarnocki-Cieciura M, Dziembowski A, Orłowski M, Tkocz K, Ożyhar A
RgGuinier 5.7 nm
Dmax 22.0 nm
VolumePorod 275 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