Browse by ORGANISM: Escherichia coli

SASDGV6 – Cysteine synthase A

Cysteine synthase A experimental SAS data
DAMMIN model
Sample: Cysteine synthase A dimer, 71 kDa Escherichia coli protein
Buffer: 20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE, pH: 7.5
Experiment: SAXS data collected at Austrian SAXS beamline 5.2L, ELETTRA on 2016 Jun 1
Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action. Int J Mol Sci 20(20) (2019)
Rosa B, Marchetti M, Paredi G, Amenitsch H, Franko N, Benoni R, Giabbai B, De Marino MG, Mozzarelli A, Ronda L, Storici P, Campanini B, Bettati S
RgGuinier 2.6 nm
Dmax 8.5 nm
VolumePorod 108 nm3

SASDGW6 – Serine acetyltransferase

Serine acetyltransferase experimental SAS data
DAMMIF model
Sample: Serine acetyltransferase hexamer, 177 kDa Escherichia coli protein
Buffer: 20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE, pH: 7.5
Experiment: SAXS data collected at Austrian SAXS beamline 5.2L, ELETTRA on 2016 Jun 1
Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action. Int J Mol Sci 20(20) (2019)
Rosa B, Marchetti M, Paredi G, Amenitsch H, Franko N, Benoni R, Giabbai B, De Marino MG, Mozzarelli A, Ronda L, Storici P, Campanini B, Bettati S
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 280 nm3

SASDGX6 – Cysteine synthase/Serine acetyltransferase complex

Cysteine synthase A (4-mer)Serine acetyltransferase (6-mer) experimental SAS data
DAMMIF model
Sample: Cysteine synthase A (4-mer) tetramer, 143 kDa Escherichia coli protein
Serine acetyltransferase (6-mer) hexamer, 177 kDa Escherichia coli protein
Buffer: 20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE, pH: 7.5
Experiment: SAXS data collected at Austrian SAXS beamline 5.2L, ELETTRA on 2016 Jun 1
Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action. Int J Mol Sci 20(20) (2019)
Rosa B, Marchetti M, Paredi G, Amenitsch H, Franko N, Benoni R, Giabbai B, De Marino MG, Mozzarelli A, Ronda L, Storici P, Campanini B, Bettati S
RgGuinier 6.1 nm
Dmax 22.0 nm
VolumePorod 457 nm3

SASDGN2 – F670E mutated dimeric bifunctional alcohol/aldehyde dehydrogenase

F670E Aldehyde-alcohol dehydrogenase experimental SAS data
SREFLEX model
Sample: F670E Aldehyde-alcohol dehydrogenase dimer, 192 kDa Escherichia coli protein
Buffer: 50 mM HEPES pH 7, 500 mM NaCl, 5% (v/v) glycerol, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Oct 4
Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity. Nat Commun 10(1):4527 (2019)
Kim G, Azmi L, Jang S, Jung T, Hebert H, Roe AJ, Byron O, Song JJ
RgGuinier 5.0 nm
Dmax 17.4 nm
VolumePorod 260 nm3

SASDFB6 – The periplasmically localised protease PqqL from Escherichia coli

Zinc protease PqqL experimental SAS data
DAMMIF model
Sample: Zinc protease PqqL monomer, 102 kDa Escherichia coli protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jun 14
Protease-associated import systems are widespread in Gram-negative bacteria. PLoS Genet 15(10):e1008435 (2019)
Grinter R, Leung PM, Wijeyewickrema LC, Littler D, Beckham S, Pike RN, Walker D, Greening C, Lithgow T
RgGuinier 4.0 nm
Dmax 13.7 nm
VolumePorod 207 nm3

SASDGL2 – Ring opening PaaZ from the phenylacetate degradation pathway (E. coli K12)

Bifunctional protein PaaZ experimental SAS data
OTHER model
Sample: Bifunctional protein PaaZ hexamer, 438 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 50 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Feb 24
Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway. Nat Commun 10(1):4127 (2019)
Sathyanarayanan N, Cannone G, Gakhar L, Katagihallimath N, Sowdhamini R, Ramaswamy S, Vinothkumar KR
RgGuinier 6.2 nm
Dmax 20.0 nm
VolumePorod 636 nm3

SASDFD8 – Histidine-binding periplasmic protein (HisBP), apo-form

Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 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 2.0 nm
Dmax 6.0 nm
VolumePorod 32 nm3

SASDFE8 – Histidine-binding periplasmic protein (HisBP) in the presence of histidine - His-bound 5-fold excess

Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 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 1.8 nm
Dmax 5.7 nm
VolumePorod 33 nm3

SASDFF8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP), apo-form

Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 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 6.2 nm
VolumePorod 35 nm3

SASDFG8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP) in the presence of glutamine - Gln-bound 10-fold excess

Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 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 2.0 nm
Dmax 6.1 nm
VolumePorod 34 nm3