SASDAU5 – ad11 Fab + NGF

aD11 FabNGF experimental SAS data
DAMMIN model
Sample: aD11 Fab dimer, 50 kDa Mus musculus protein
NGF dimer, 50 kDa Mus musculus protein
Buffer: 30 mM Na-phosphate 75 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III on 2005 Dec 20
Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody. J Mol Biol 381(4):881-96 (2008)
Covaceuszach S, Cassetta A, Konarev PV, Gonfloni S, Rudolph R, Svergun DI, Lamba D, Cattaneo A
RgGuinier 4.3 nm
Dmax 16.0 nm
VolumePorod 255 nm3

SASDLX4 – Full-length flavorubredoxin

Anaerobic nitric oxide reductase flavorubredoxin experimental SAS data
Full-length flavorubredoxin Rg histogram
Sample: Anaerobic nitric oxide reductase flavorubredoxin tetramer, 217 kDa Escherichia coli (strain … protein
Buffer: 50 mM Tris-HCl, 18% glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Nov 19
Quaternary Structure of Flavorubredoxin as Revealed by Synchrotron Radiation Small-Angle X-Ray Scattering Structure 16(9):1428-1436 (2008)
Petoukhov M, Vicente J, Crowley P, Carrondo M, Teixeira M, Svergun D
RgGuinier 4.1 nm
Dmax 14.2 nm
VolumePorod 297 nm3

SASDA94 – Der p21

Der p21, allegren experimental SAS data
DAMMIN model
Sample: Der p21, allegren dimer, 26 kDa Escherichia coli protein
Buffer: 10 mM Hepes , pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Jul 24
Characterization of Der p 21, a new important allergen derived from the gut of house dust mites. Allergy 63(6):758-67 (2008)
Weghofer M, Dall'Antonia Y, Grote M, Stöcklinger A, Kneidinger M, Balic N, Krauth MT, Fernández-Caldas E, Thomas WR, van Hage M, Vieths S, Spitzauer S, Horak F, Svergun DI, Konarev PV, Valent P, Thalh...
RgGuinier 2.7 nm
Dmax 8.5 nm
VolumePorod 50 nm3

SASDAN5 – Cross-linked complex CytC_Adr

Cytochrome CAdrenodoxin experimental SAS data
DAMMIN model
Sample: Cytochrome C monomer, 11 kDa Escherichia coli protein
Adrenodoxin monomer, 11 kDa Escherichia coli protein
Buffer: 20 mM HEPES 2 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Jun 15
Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy. J Am Chem Soc 130(20):6395-403 (2008)
Xu X, Reinle W, Hannemann F, Konarev PV, Svergun DI, Bernhardt R, Ubbink M
RgGuinier 2.1 nm
Dmax 8.5 nm
VolumePorod 42 nm3

SASDAP5 – Native complex CytC_Adr

Cytochrome C dimerAdrenodoxin dimer experimental SAS data
DAMMIN model
Sample: Cytochrome C dimer dimer, 22 kDa Escherichia coli protein
Adrenodoxin dimer dimer, 22 kDa Escherichia coli protein
Buffer: 20 mM HEPES 2 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Jun 15
Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy. J Am Chem Soc 130(20):6395-403 (2008)
Xu X, Reinle W, Hannemann F, Konarev PV, Svergun DI, Bernhardt R, Ubbink M
RgGuinier 2.9 nm
Dmax 9.5 nm
VolumePorod 64 nm3

SASDAN4 – Calmodulin:peptide complex

CalmodulinC-terminal region of human myelin basic protein experimental SAS data
SASREF model
Sample: Calmodulin monomer, 17 kDa Homo sapiens protein
C-terminal region of human myelin basic protein monomer, 2 kDa Homo sapiens protein
Buffer: 25 mM Tris75 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Nov 28
Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure. BMC Struct Biol 8:10 (2008)
Majava V, Petoukhov MV, Hayashi N, Pirilä P, Svergun DI, Kursula P
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 36 nm3

SASDAK5 – Myomesin-1 My12-My13

Myomesin-1 experimental SAS data
CRYSOL model
Sample: Myomesin-1 dimer, 46 kDa Homo sapiens protein
Buffer: 25 mM Tris/HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2005 May 7
Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin. EMBO J 27(1):253-64 (2008)
Pinotsis N, Lange S, Perriard JC, Svergun DI, Wilmanns M
RgGuinier 4.0 nm
Dmax 14.5 nm
VolumePorod 56 nm3

SASDH43 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.2 nm
Dmax 10.0 nm
VolumePorod 135 nm3

SASDH53 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with calcium

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 160 nm3

SASDH63 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, 0.25 mM IP3, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.1 nm
Dmax 8.8 nm
VolumePorod 115 nm3

2004 hits found.