Browse by ORGANISM: Escherichia coli

SASDFH8 – Glutamate/aspartate import solute-binding protein (DEBP), apo-form

Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.3 nm
Dmax 8.5 nm
VolumePorod 44 nm3

SASDFJ8 – Glutamate/aspartate import solute-binding protein (DEBP) in the presence of glutamate - Glu-bound 10-fold excess

Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.1 nm
Dmax 6.4 nm
VolumePorod 39 nm3

SASDDY9 – Protein translocase subunit SecA (full length, amino acids 1-901)

Protein translocase subunit SecA experimental SAS data
Protein translocase subunit SecA Kratky plot
Sample: Protein translocase subunit SecA dimer, 204 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, 1mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 18
The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. Elife 8 (2019)
Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D
RgGuinier 4.2 nm
Dmax 14.9 nm
VolumePorod 424 nm3

SASDDZ9 – Protein translocase subunit SecA (amino acids 1-880)

Protein translocase subunit SecA experimental SAS data
Protein translocase subunit SecA Kratky plot
Sample: Protein translocase subunit SecA dimer, 199 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, 1mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 18
The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. Elife 8 (2019)
Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D
RgGuinier 4.2 nm
Dmax 14.8 nm
VolumePorod 380 nm3

SASDE22 – Protein translocase subunit SecA (amino acids 1-832)

Protein translocase subunit SecA experimental SAS data
Protein translocase subunit SecA Kratky plot
Sample: Protein translocase subunit SecA dimer, 189 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, 1mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 18
The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. Elife 8 (2019)
Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D
RgGuinier 4.5 nm
Dmax 15.7 nm
VolumePorod 398 nm3

SASDEL9 – Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaFatty acid oxidation complex subunit alpha3-ketoacyl-CoA thiolase FadA (beta subunit) experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
3-ketoacyl-CoA thiolase FadA (beta subunit) dimer, 82 kDa Escherichia coli protein
Buffer: 20 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 120 mM KCl, 2.5 mM DTT, pH: 7.2
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 30
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 406 nm3

SASDEM9 – anEcTFE: Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic 3-ketoacyl-CoA thiolase FadI beta subunitanaerobic 3-ketoacyl-CoA thiolase FadI beta subunit experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli (strain … protein
Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
Anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
Anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
Buffer: 50 mM Tris, 500 mM NaCl, 5% glycerol, 0.05% C12E9 (1-O-(n-Dodecyl)-nonaethyleneglycol), 2.5 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 22
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 6.2 nm
Dmax 19.6 nm
VolumePorod 856 nm3

SASDKD4 – In vitro DNA protection during starvation protein (Dps)/DNA co-crystallization

DNA protection during starvation protein experimental SAS data
DNA protection during starvation protein Kratky plot
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM EDTA, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 27
Protective Dps-DNA co-crystallization in stressed cells: an in vitro structural study by small-angle X-ray scattering and cryo-electron tomography. FEBS Lett 593(12):1360-1371 (2019)
Dadinova LA, Chesnokov YM, Kamyshinsky RA, Orlov IA, Petoukhov MV, Mozhaev AA, Soshinskaya EY, Lazarev VN, Manuvera VA, Orekhov AS, Vasiliev AL, Shtykova EV

SASDFR4 – HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli (Domain A (PDB:3MLI)-Linker (PDB:1BR0)-Domain B (PDB:1WRT))

HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli experimental SAS data
CORAL model
Sample: HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli tetramer, 150 kDa Helicobacter pylori, Rattus … protein
Buffer: 20 mM Tris-HCl 150 mM NaCl, pH: 8
Experiment: SAXS data collected at Rigaku Nano-Viewer, Nara Institute of Science and Technology on 2016 Dec 8
Construction of a Quadrangular Tetramer and a Cage-Like Hexamer from Three-Helix Bundle-Linked Fusion Proteins. ACS Synth Biol (2019)
Miyamoto T, Hayashi Y, Yoshida K, Watanabe H, Uchihashi T, Yonezawa K, Shimizu N, Kamikubo H, Hirota S
RgGuinier 5.1 nm
Dmax 20.0 nm
VolumePorod 379 nm3

SASDKM7 – Sulfite reductase flavoprotein-60

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS (BL-6), Spallation Neutron Source on 2018 Jul 11
NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase Journal of Structural Biology 205(2):170-179 (2019)
Tavolieri A, Murray D, Askenasy I, Pennington J, McGarry L, Stanley C, Stroupe M
RgGuinier 3.2 nm
Dmax 11.6 nm
VolumePorod 60 nm3