Browse by ORGANISM: Escherichia coli

SASDJ28 – Ferric Iron Reductase - FhuF∆1-17

Ferric iron reductase protein FhuF (∆1-17) experimental SAS data
DAMFILT model
Sample: Ferric iron reductase protein FhuF (∆1-17) monomer, 28 kDa Escherichia coli (strain … protein
Buffer: 20 mM Phosphate, 200 mM NaCl, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Apr 16
Conjuring up a ghost: structural and functional characterization of FhuF, a ferric siderophore reductase from E. coli JBIC Journal of Biological Inorganic Chemistry (2021)
Trindade I, Hernandez G, Lebègue E, Barrière F, Cordeiro T, Piccioli M, Louro R
RgGuinier 2.1 nm
Dmax 8.8 nm
VolumePorod 60 nm3

SASDJ84 – Intimin D00-D0 domain

Intimin, D00-D0 domain (6xHis tagged) experimental SAS data
EOM/RANCH model
Sample: Intimin, D00-D0 domain (6xHis tagged) monomer, 23 kDa Escherichia coli O127:H6 … protein
Buffer: 10 mM HEPES, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 12
The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action. Sci Rep 10(1):21249 (2020)
Weikum J, Kulakova A, Tesei G, Yoshimoto S, Jægerum LV, Schütz M, Hori K, Skepö M, Harris P, Leo JC, Morth JP
RgGuinier 3.1 nm
Dmax 8.3 nm
VolumePorod 32 nm3

SASDJ94 – Intimin D0-D1 domain

Intimin (D0-D1 domain, 6xHis tagged) experimental SAS data
Intimin D0-D1 domain Rg histogram
Sample: Intimin (D0-D1 domain, 6xHis tagged) monomer, 23 kDa Escherichia coli O127:H6 … protein
Buffer: 10 mM HEPES, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 12
The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action. Sci Rep 10(1):21249 (2020)
Weikum J, Kulakova A, Tesei G, Yoshimoto S, Jægerum LV, Schütz M, Hori K, Skepö M, Harris P, Leo JC, Morth JP
RgGuinier 2.2 nm
Dmax 5.8 nm
VolumePorod 34 nm3

SASDJT4 – Complex of Candidatus Glomeribacter gigasporarum cyclodipeptide synthase (Cglo-CDPS) with Phe-tRNAPhe

Candidatus Glomeribacter gigasporarum cyclodipeptide synthaseE. coli Phe-tRNAPhe experimental SAS data
Candidatus Glomeribacter gigasporarum cyclodipeptide synthase E. coli Phe-tRNAPhe Kratky plot
Sample: Candidatus Glomeribacter gigasporarum cyclodipeptide synthase monomer, 34 kDa Candidatus Glomeribacter gigasporarum protein
E. coli Phe-tRNAPhe monomer, 25 kDa Escherichia coli RNA
Buffer: 10 mM MOPS pH6.7; 200 mM NaCl, 8 mM MgCl2, pH: 6.7
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Oct 2
Structural basis of the interaction between cyclodipeptide synthases and aminoacylated tRNA substrates. RNA 26(11):1589-1602 (2020)
Bourgeois G, Seguin J, Babin M, Gondry M, Mechulam Y, Schmitt E
RgGuinier 3.3 nm
Dmax 14.0 nm
VolumePorod 77 nm3

SASDC72 – Alcohol dehydrogenase from bifunctional alcohol/aldehyde dehydrogenase (P0A9Q8)

Aldehyde-alcohol dehydrogenase experimental SAS data
DAMMIF model
Sample: Aldehyde-alcohol dehydrogenase dimer, 97 kDa Escherichia coli O157:H7 protein
Buffer: 20 mM Tris 400 mM NaCl 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2015 Nov 27
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE. Acta Crystallogr F Struct Biol Commun 76(Pt 9):414-421 (2020)
Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M
RgGuinier 3.2 nm
Dmax 16.9 nm
VolumePorod 146 nm3

SASDCK3 – Aldehyde dehydrogenase

Aldehyde-alcohol dehydrogenase experimental SAS data
DAMMIF model
Sample: Aldehyde-alcohol dehydrogenase monomer, 48 kDa Escherichia coli O157:H7 protein
Buffer: 30 mM HEPES, 150 mM NaCl, 5% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jan 30
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE. Acta Crystallogr F Struct Biol Commun 76(Pt 9):414-421 (2020)
Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M
RgGuinier 2.7 nm
Dmax 11.1 nm
VolumePorod 74 nm3

SASDJA4 – Endonuclease VIII from E. coli (size exclusion chromatography SAXS)

Endonuclease 8 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Endonuclease 8 monomer, 31 kDa Escherichia coli protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, 2% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Mar 9
Unique Structural Features of Mammalian NEIL2 DNA Glycosylase Prime Its Activity for Diverse DNA Substrates and Environments. Structure (2020)
Eckenroth BE, Cao VB, Averill AM, Dragon JA, Doublié S
RgGuinier 2.3 nm
Dmax 7.8 nm
VolumePorod 45 nm3

SASDFP5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 7.5 with 50 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 16-mer, 153 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 8.9 nm
Dmax 28.5 nm
VolumePorod 410 nm3

SASDFQ5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 7.5 with 100 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 16-mer, 153 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.6 nm
Dmax 25.0 nm
VolumePorod 336 nm3

SASDFR5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 7.5 with 150 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 14-mer, 133 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 5.8 nm
Dmax 24.2 nm
VolumePorod 308 nm3