SASDGM5 – Holo-RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA)

RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) experimental SAS data
OTHER model
Sample: RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) monomer, 73 kDa Bordetella pertussis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM DTT, 4 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 May 31
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion. Sci Rep 5:14223 (2015)
O'Brien DP, Hernandez B, Durand D, Hourdel V, Sotomayor-Pérez AC, Vachette P, Ghomi M, Chamot-Rooke J, Ladant D, Brier S, Chenal A
RgGuinier 4.4 nm
Dmax 15.5 nm
VolumePorod 89 nm3

SASDGN5 – apo-RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA)

RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) experimental SAS data
OTHER model
Sample: RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) monomer, 73 kDa Bordetella pertussis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 May 31
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion. Sci Rep 5:14223 (2015)
O'Brien DP, Hernandez B, Durand D, Hourdel V, Sotomayor-Pérez AC, Vachette P, Ghomi M, Chamot-Rooke J, Ladant D, Brier S, Chenal A
RgGuinier 8.3 nm
Dmax 33.0 nm

SASDCH2 – Aldehyde dehydrogenase 7A1

Aldehyde dehydrogenase 7A1 (Alpha-aminoadipic semialdehyde dehydrogenase) experimental SAS data
NONE model
Sample: Aldehyde dehydrogenase 7A1 (Alpha-aminoadipic semialdehyde dehydrogenase) tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 9
Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1. Biochemistry 54(35):5513-22 (2015)
Luo M, Tanner JJ
RgGuinier 3.8 nm
Dmax 11.5 nm
VolumePorod 270 nm3

SASDAR6 – human CSF-1:CSF-1R extracellular signalling complex

Macrophage colony-stimulating factor 1Macrophage colony-stimulating factor 1 receptor experimental SAS data
SASREF model
Sample: Macrophage colony-stimulating factor 1 dimer, 35 kDa Homo sapiens protein
Macrophage colony-stimulating factor 1 receptor dimer, 107 kDa Homo sapiens protein
Buffer: 50 mM NaH2PO4, 100 m, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Mar 13
Structure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1. Structure 23(9):1621-1631 (2015)
Felix J, De Munck S, Verstraete K, Meuris L, Callewaert N, Elegheert J, Savvides SN
RgGuinier 5.7 nm
Dmax 17.9 nm
VolumePorod 299 nm3

SASDA28 – anti-TG2 antibody (679 14 E06)

anti-TG2 antibody (679 14 E06) experimental SAS data
CRYSOL model
Sample: anti-TG2 antibody (679 14 E06) monomer, 48 kDa protein
Buffer: 20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17
Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease. J Biol Chem 290(35):21365-75 (2015)
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM
RgGuinier 2.5 nm
Dmax 8.1 nm
VolumePorod 58 nm3

SASDA38 – transglutaminase-2 (TGA2)

transglutaminase 2 experimental SAS data
CRYSOL model
Sample: transglutaminase 2 monomer, 79 kDa Homo sapiens protein
Buffer: 20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17
Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease. J Biol Chem 290(35):21365-75 (2015)
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 117 nm3

SASDA48 – transglutaminase2:anti-transglutaminase2 FAB1 antibody complex

anti-TG2 antibody (679 14 E06) transglutaminase 2 experimental SAS data
DAMMIN model
Sample: anti-TG2 antibody (679 14 E06) monomer, 48 kDa protein
transglutaminase 2 monomer, 79 kDa Homo sapiens protein
Buffer: 20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17
Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease. J Biol Chem 290(35):21365-75 (2015)
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM
RgGuinier 4.0 nm
Dmax 13.9 nm
VolumePorod 168 nm3

SASDCJ2 – Solution structure of recombinant prion protein (89–230) in complex with Fab-P

Major prion proteinP-Clone Fab, Chimera experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Major prion protein monomer, 23 kDa Mus musculus protein
P-Clone Fab, Chimera monomer, 47 kDa Homo sapiens protein
Buffer: sodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl), pH: 5.1
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2013 Dec 5
Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophys J 109(4):793-805 (2015)
Carter L, Kim SJ, Schneidman-Duhovny D, Stöhr J, Poncet-Montange G, Weiss TM, Tsuruta H, Prusiner SB, Sali A
RgGuinier 3.9 nm
Dmax 14.5 nm
VolumePorod 106 nm3

SASDAG7 – CD44 HABD scFv MEM-85 complex

Hyaluronate binding domain of CD44 antigenSingle-chain Variable Fragment of Antibody MEM-85 experimental SAS data
DAMMIN model
Sample: Hyaluronate binding domain of CD44 antigen monomer, 18 kDa Homo sapiens protein
Single-chain Variable Fragment of Antibody MEM-85 monomer, 29 kDa Mus musculus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Molecular mechanism for the action of the anti-CD44 monoclonal antibody MEM-85. J Struct Biol 191(2):214-23 (2015)
Škerlová J, Král V, Kachala M, Fábry M, Bumba L, Svergun DI, Tošner Z, Veverka V, Řezáčová P
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 57 nm3

SASDAD8 – Antiapoptotic membrane protein, (DpV84gp022) Deerpox virus

Antiapoptotic membrane protein experimental SAS data
Antiapoptotic membrane protein Kratky plot
Sample: Antiapoptotic membrane protein dimer, 39 kDa Deerpox virus W-1170-84 protein
Buffer: 25 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2013 May 4
Structural basis of Deerpox virus-mediated inhibition of apoptosis. Acta Crystallogr D Biol Crystallogr 71(Pt 8):1593-603 (2015)
Burton DR, Caria S, Marshall B, Barry M, Kvansakul M
RgGuinier 2.6 nm
Dmax 11.1 nm
VolumePorod 61 nm3

4706 hits found.