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

SASDFT9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S2 (-ss) ECR

Adhesion G-protein coupled receptor G6 S2 experimental SAS data
Adhesion G-protein coupled receptor G6 S2 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 monomer, 86 kDa Danio rerio protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.0 nm
Dmax 14.1 nm
VolumePorod 169 nm3

SASDFU9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S1 (+ss) ECR

Adhesion G-protein coupled receptor G6 S1 experimental SAS data
Adhesion G-protein coupled receptor G6 S1 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S1 monomer, 89 kDa Danio rerio protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.2 nm
Dmax 14.8 nm
VolumePorod 191 nm3

SASDFV9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S2 (-ss) D134A/F135A ECR

Adhesion G-protein coupled receptor G6 S2 D134A/F135A experimental SAS data
Adhesion G-protein coupled receptor G6 S2 D134A/F135A Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 D134A/F135A monomer, 86 kDa Danio rerio protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.3 nm
Dmax 14.8 nm
VolumePorod 181 nm3

SASDFW9 – Adhesion G-protein coupled receptor G6 - hGPR126 S2 (-ss) ECR

Adhesion G-protein coupled receptor G6 S2 experimental SAS data
Adhesion G-protein coupled receptor G6 S2 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 monomer, 88 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.4 nm
Dmax 15.7 nm
VolumePorod 199 nm3

SASDFX9 – Adhesion G-protein coupled receptor G6 - hGPR126 S1 (+ss) ECR

Adhesion G-protein coupled receptor G6 S1 experimental SAS data
Adhesion G-protein coupled receptor G6 S1 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S1 monomer, 91 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.9 nm
Dmax 17.1 nm
VolumePorod 213 nm3

SASDGB6 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8A) miniGi complex

Resistance to inhibitors of cholinesterase 8 homolog AminiGi experimental SAS data
OTHER model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Bos taurus protein
miniGi monomer, 25 kDa synthetic construct protein
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Oct 27
Large-scale conformational rearrangement of the α5-helix of Gα subunits in complex with the guanine nucleotide exchange factor Ric8A. J Biol Chem (2019)
Srivastava D, Artemyev NO
RgGuinier 3.2 nm
Dmax 10.7 nm

SASDFL6 – Adenine specific DNA methyltransferase (Mod Hp_0593) at pH 8

Adenine specific DNA methyltransferase (Mod) experimental SAS data
PYMOL model
Sample: Adenine specific DNA methyltransferase (Mod) dimer, 137 kDa Helicobacter pylori protein
Buffer: 25 mM Tris, 250 mM NaCl, pH: 8
Experiment: SAXS data collected at ID14-3, ESRF on 2017 Jul 9
Tetramerization at low pH licenses DNA methylation activity of M.HpyAXI in the presence of acid stress. J Mol Biol (2019)
Narayanan N, Banerjee A, Jain D, Kulkarni DS, Sharma R, Nirwal S, Rao DN, Nair DT
RgGuinier 3.3 nm
Dmax 12.5 nm
VolumePorod 143 nm3

SASDFM6 – Adenine specific DNA methyltransferase (Mod HP_0593) at pH 5.5

Adenine specific DNA methyltransferase (Mod) experimental SAS data
PYMOL model
Sample: Adenine specific DNA methyltransferase (Mod) tetramer, 273 kDa Helicobacter pylori protein
Buffer: 25 mM citrate, 250 mM NaCl, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Dec 1
Tetramerization at low pH licenses DNA methylation activity of M.HpyAXI in the presence of acid stress. J Mol Biol (2019)
Narayanan N, Banerjee A, Jain D, Kulkarni DS, Sharma R, Nirwal S, Rao DN, Nair DT
RgGuinier 5.0 nm
Dmax 19.1 nm
VolumePorod 316 nm3

SASDFA6 – Proteolytic fragment of phage flagella binding tail protein YSD1_29 (amino acids 373-1296)

Flagella binding tail protein experimental SAS data
DAMMIF model
Sample: Flagella binding tail protein monomer, 103 kDa Salmonella virus Chi protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 4
The flagellotropic bacteriophage YSD1 targets Salmonella Typhi with a Chi-like protein tail fibre. Mol Microbiol (2019)
Dunstan RA, Pickard D, Dougan S, Goulding D, Cormie C, Hardy J, Li F, Grinter R, Harcourt K, Yu L, Song J, Schreiber F, Choudhary J, Clare S, Coulibaly F, Strugnell RA, Dougan G, Lithgow T
RgGuinier 5.6 nm
Dmax 27.4 nm
VolumePorod 155 nm3

4122 hits found.