Browse by ORGANISM: Escherichia coli

SASDAA9 – EcPaaA2-EcParE2His construct

Plasmid stabilization protein ParE Uncharacterized protein (Antitoxin) experimental SAS data
CRYSOL model
Sample: Plasmid stabilization protein ParE 16-mer, 188 kDa Escherichia coli protein
Uncharacterized protein (Antitoxin) 16-mer, 135 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 9
A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. J Mol Biol 428(8):1589-603 (2016)
Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R
RgGuinier 3.8 nm
Dmax 16.2 nm
VolumePorod 312 nm3

SASDAB9 – EcPaaA2-HisEcParE2 construct

Plasmid stabilization protein ParEUncharacterized protein (Antitoxin) experimental SAS data
CRYSOL model
Sample: Plasmid stabilization protein ParE octamer, 102 kDa Escherichia coli protein
Uncharacterized protein (Antitoxin) octamer, 68 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 Feb 5
A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. J Mol Biol 428(8):1589-603 (2016)
Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R
RgGuinier 3.3 nm
Dmax 15.3 nm
VolumePorod 166 nm3

SASDC84 – parDE-like toxin-antitoxin module, EcPaaA2_13-63-HisEcParE2 construct

Plasmid stabilization protein ParEUncharacterized protein experimental SAS data
parDE-like toxin-antitoxin module, EcPaaA2_13-63-HisEcParE2 construct Rg histogram
Sample: Plasmid stabilization protein ParE monomer, 13 kDa Escherichia coli protein
Uncharacterized protein monomer, 6 kDa Escherichia coli O157:H7 protein
Buffer: 50 mM Tris-HCl, 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 Feb 5
A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. J Mol Biol 428(8):1589-603 (2016)
Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R
RgGuinier 2.2 nm
Dmax 9.3 nm
VolumePorod 36 nm3

SASDBY2 – Inorganic pyrophosphatase (PPase) from E. coli

Inorganic pyrophosphatase (PPase) from E. coli experimental SAS data
DAMMIN model
Sample: Inorganic pyrophosphatase (PPase) from E. coli hexamer, 117 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 3.0 nm
Dmax 9.0 nm
VolumePorod 166 nm3

SASDBZ2 – Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli

Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli experimental SAS data
DAMMIN model
Sample: Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli decamer, 381 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.4 nm
Dmax 12.7 nm
VolumePorod 484 nm3

SASDB23 – 5-keto-4-deoxyuronate isomerase (KduI) from E. coli

5-keto-4-deoxyuronate isomerase (KduI) from E. coli experimental SAS data
NONE model
Sample: 5-keto-4-deoxyuronate isomerase (KduI) from E. coli None, Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 20
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.5 nm

SASDB33 – Glutamate decarboxylase alpha (GadA) from E. coli

Glutamate decarboxylase alpha (GadA) from E. coli experimental SAS data
SASREF MX model
Sample: Glutamate decarboxylase alpha (GadA) from E. coli monomer, 53 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 20
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.8 nm
VolumePorod 410 nm3

SASDBS4 – Glutamate decarboxylase alpha (GadA) from E. coli, low salt

Glutamate decarboxylase alpha (GadA) from E. coli experimental SAS data
SASREF MX model
Sample: Glutamate decarboxylase alpha (GadA) from E. coli monomer, 53 kDa Escherichia coli protein
Buffer: 50 mM Tris, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jul 29
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.4 nm
VolumePorod 450 nm3

SASDAH6 – WbdD(1-459)

bifunctional kinase- methyltransferase WbdD experimental SAS data
CORAL model
Sample: Bifunctional kinase- methyltransferase WbdD monomer, 59 kDa Escherichia coli protein
Buffer: 20 mM BisTris 50 mM NaCl 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Sep 23
A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide. Nat Struct Mol Biol 22(1):50-56 (2015)
Hagelueken G, Clarke BR, Huang H, Tuukkanen A, Danciu I, Svergun DI, Hussain R, Liu H, Whitfield C, Naismith JH
RgGuinier 3.1 nm
Dmax 10.0 nm
VolumePorod 90 nm3

SASDH23 – Antigen 43 alpha domain

Alpha domain of Ag43a experimental SAS data
DAMMIN model
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2009 Nov 19
The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping. Proc Natl Acad Sci U S A 111(1):457-62 (2014)
Heras B, Totsika M, Peters KM, Paxman JJ, Gee CL, Jarrott RJ, Perugini MA, Whitten AE, Schembri MA
RgGuinier 3.6 nm
Dmax 12.2 nm
VolumePorod 62 nm3