Browse by ORGANISM: Escherichia coli

SASDA65 – Nucleoplasmin-H5 complex

NP-H5 experimental SAS data
MONSA model
Sample: NP-H5 pentamer, 200 kDa Escherichia coli protein
Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 3
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
Taneva SG, Bañuelos S, Falces J, Arregi I, Muga A, Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA
RgGuinier 5.2 nm
Dmax 16.7 nm
VolumePorod 410 nm3

SASDA75 – Nucleoplasmin-H2AH2B complex

NP-H2AH2B experimental SAS data
MONSA model
Sample: NP-H2AH2B pentamer, 250 kDa Escherichia coli protein
Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2014 Dec 3
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
Taneva SG, Bañuelos S, Falces J, Arregi I, Muga A, Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA
RgGuinier 4.7 nm
Dmax 14.5 nm
VolumePorod 470 nm3

SASDAS3 – Fila16-17

immunoglobulin- like filamin two-domain fragment 16-17 experimental SAS data
GASBOR model
Sample: Immunoglobulin- like filamin two-domain fragment 16-17 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 33 nm3

SASDAT3 – Fila18-19

immunoglobulin- like filamin two-domain fragment 18-19 experimental SAS data
GASBOR model
Sample: Immunoglobulin- like filamin two-domain fragment 18-19 monomer, 20 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 34 nm3

SASDAU3 – Fila22-23

immunoglobulin- like filamin two-domain fragment 22-23 experimental SAS data
GASBOR model
Sample: Immunoglobulin- like filamin two-domain fragment 22-23 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 32 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, DESY 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, DESY 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, Thalhamer J, Keller W, Valenta R, Vrtala S
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, DESY 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, DESY 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

SASDAC4 – FilaminC 23-24

Filamin C 23-24 experimental SAS data
DAMMIN model
Sample: Filamin C 23-24 dimer, 40 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jun 17
Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol 368(4):1011-23 (2007)
Sjekloća L, Pudas R, Sjöblom B, Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylänne J, Djinović Carugo K
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 75 nm3