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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

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

SASDG26 – Wild type 4-hydroxy-tetrahydrodipicolinate synthase

4-hydroxy-tetrahydrodipicolinate synthase experimental SAS data
DAMFILT model
Sample: 4-hydroxy-tetrahydrodipicolinate synthase tetramer, 131 kDa Campylobacter jejuni protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Aug 2
Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase. J Struct Biol :107409 (2019)
Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ
RgGuinier 3.4 nm
Dmax 9.0 nm
VolumePorod 188 nm3

SASDG36 – 4-hydroxy-tetrahydrodipicolinate synthase (N84D mutant)

4-hydroxy-tetrahydrodipicolinate synthase (N84D mutant) experimental SAS data
DAMFILT model
Sample: 4-hydroxy-tetrahydrodipicolinate synthase (N84D mutant) dimer, 65 kDa Campylobacter jejuni protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Aug 2
Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase. J Struct Biol :107409 (2019)
Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ
RgGuinier 3.1 nm
Dmax 9.5 nm
VolumePorod 108 nm3

SASDG46 – 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant)

4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant) experimental SAS data
DAMFILT model
Sample: 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant), 33 kDa Campylobacter jejuni protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Aug 2
Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase. J Struct Biol :107409 (2019)
Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ
RgGuinier 3.3 nm
Dmax 8.9 nm
VolumePorod 163 nm3

SASDH25 – Actinobacterial phosphodiesterase targeting cyclic di-AMP (AtaC)

Alkaline phosphodiesterase I or Nucleotide pyrophosphatase experimental SAS data
Alkaline phosphodiesterase I or Nucleotide pyrophosphatase Kratky plot
Sample: Alkaline phosphodiesterase I or Nucleotide pyrophosphatase monomer, 46 kDa Streptomyces venezuelae protein
Buffer: 20 mM HEPES, 200mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 17
c-di-AMP hydrolysis by a novel type of phosphodiesterase promotes differentiation of multicellular bacteria (2019)
Latoscha A, Drexler D, Al-Bassam M, Kaever V, Findlay K, Witte G, Tschowri N
RgGuinier 2.4 nm
Dmax 7.8 nm
VolumePorod 74 nm3