SASBDB entries for UniProt ID:

SASDE58 – Complex of toxin GraT with antotoxin GraA

UniProt ID: Q88MI5 (1-91) Putative killer protein, Toxin GraT.

UniProt ID: Q88MI6 (1-99) antitoxin GraA, antidote of toxin GraT

UniProt ID: None (1-91) Putative killer protein, Toxin GraT
Putative killer protein, Toxin GraT.antitoxin GraA, antidote of toxin GraTPutative killer protein, Toxin GraT experimental SAS data
Putative killer protein, Toxin GraT. antitoxin GraA, antidote of toxin GraT Putative killer protein, Toxin GraT Kratky plot
Sample: Putative killer protein, Toxin GraT. monomer, 11 kDa Pseudomonas putida protein
Antitoxin GraA, antidote of toxin GraT dimer, 22 kDa Pseudomonas putida protein
Putative killer protein, Toxin GraT monomer, 11 kDa Pseudomonas putida protein
Buffer: 50 mM Tris 250 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 29
A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. Nat Commun 10(1):972 (2019)
Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R
RgGuinier 2.3 nm
Dmax 7.9 nm
VolumePorod 63 nm3

SASDE68 – Two dimers of antitoxin GraA in complex with the grta operator

UniProt ID: None (None-None) GraTA operator region

UniProt ID: Q88MI6 (1-99) antitoxin GraA, antidote of toxin GraT

UniProt ID: Q88MI6 (1-99) atitoxin GraA, antidote of GraT.
GraTA operator regionantitoxin GraA, antidote of toxin GraTatitoxin GraA, antidote of GraT. experimental SAS data
GraTA operator region antitoxin GraA, antidote of toxin GraT atitoxin GraA, antidote of GraT. Kratky plot
Sample: GraTA operator region monomer, 20 kDa DNA
Antitoxin GraA, antidote of toxin GraT dimer, 22 kDa Pseudomonas putida protein
Atitoxin GraA, antidote of GraT. dimer, 23 kDa Pseudomonas putida protein
Buffer: 50 mM Tris 250 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Dec 17
A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. Nat Commun 10(1):972 (2019)
Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R
RgGuinier 2.9 nm
Dmax 10.3 nm
VolumePorod 94 nm3

SASDE78 – Solution structure of the diadenylate cyclase/phosphoglucosamine mutase (DacA/GlmM) complex from Staphylococcus aureus

UniProt ID: A0A0H2XIU4 (100-269) Diadenylate cyclase

UniProt ID: Q2FEX1 (None-None) Phosphoglucosamine mutase
Diadenylate cyclasePhosphoglucosamine mutase experimental SAS data
DAMFILT model
Sample: Diadenylate cyclase dimer, 39 kDa Staphylococcus aureus protein
Phosphoglucosamine mutase dimer, 99 kDa Staphylococcus aureus protein
Buffer: 30 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 7
Inhibition of the Staphylococcus aureus c-di-AMP cyclase DacA by direct interaction with the phosphoglucosamine mutase GlmM. PLoS Pathog 15(1):e1007537 (2019)
Tosi T, Hoshiga F, Millership C, Singh R, Eldrid C, Patin D, Mengin-Lecreulx D, Thalassinos K, Freemont P, Gründling A
RgGuinier 3.9 nm
Dmax 12.1 nm
VolumePorod 204 nm3

SASDE88 – Solution structure of phosphoglucosamine mutase (GlmM) from Staphylococcus aureus

UniProt ID: Q2FEX1 (None-None) Phosphoglucosamine mutase
Phosphoglucosamine mutase experimental SAS data
DAMFILT model
Sample: Phosphoglucosamine mutase dimer, 99 kDa Staphylococcus aureus protein
Buffer: 30 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 7
Inhibition of the Staphylococcus aureus c-di-AMP cyclase DacA by direct interaction with the phosphoglucosamine mutase GlmM. PLoS Pathog 15(1):e1007537 (2019)
Tosi T, Hoshiga F, Millership C, Singh R, Eldrid C, Patin D, Mengin-Lecreulx D, Thalassinos K, Freemont P, Gründling A
RgGuinier 3.7 nm
Dmax 12.5 nm
VolumePorod 134 nm3

SASDE98 – Solution structure of Diadenylate cyclase (DacA) from Staphylococcus aureus

UniProt ID: A0A0H2XIU4 (100-269) Diadenylate cyclase
Diadenylate cyclase experimental SAS data
DAMFILT model
Sample: Diadenylate cyclase dimer, 39 kDa Staphylococcus aureus protein
Buffer: 30 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 7
Inhibition of the Staphylococcus aureus c-di-AMP cyclase DacA by direct interaction with the phosphoglucosamine mutase GlmM. PLoS Pathog 15(1):e1007537 (2019)
Tosi T, Hoshiga F, Millership C, Singh R, Eldrid C, Patin D, Mengin-Lecreulx D, Thalassinos K, Freemont P, Gründling A
RgGuinier 2.6 nm
Dmax 8.6 nm
VolumePorod 57 nm3

SASDEA8 – Full length of DnaG (DNA Primase) from Bacillus subtilis

UniProt ID: P05096 (None-None) DNA primase
DNA primase experimental SAS data
CORAL model
Sample: DNA primase monomer, 69 kDa Bacillus subtilis protein
Buffer: 25 mM Tris-HCl,100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Oct 1
Full length of DnaG primase from Bacillus subtilis
Zhongchuan Liu
RgGuinier 3.7 nm
Dmax 14.5 nm
VolumePorod 119 nm3

SASDEB8 – Bacillus thuringiensis LexA repressor (Bt_LexA)

UniProt ID: A0A2B4EEI3 (1-210) Bacillus thuringiensis LexA repressor
Bacillus thuringiensis LexA repressor experimental SAS data
CHIMERA model
Sample: Bacillus thuringiensis LexA repressor dimer, 47 kDa Bacillus thuringiensis protein
Buffer: 20 mM Hepes, 300 mM NaCl, 10% glycerol,, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-2000, University of British Columbia on 2017 Aug 25
Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor. Structure 27(7):1094-1102.e4 (2019)
Caveney NA, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka NCJ
RgGuinier 3.7 nm
VolumePorod 110 nm3

SASDEC8 – Bacillus thuringiensis LexA repressor bound to Bacteriophage pGIL01 gp7 (Bt_LexA_GIL01_gp7)

UniProt ID: A0A2B4EEI3 (1-210) Bacillus thuringiensis LexA repressor

UniProt ID: Q7WSG2 (1-50) Bacteriophage pGIL01 gp7
Bacillus thuringiensis LexA repressorBacteriophage pGIL01 gp7 experimental SAS data
CHIMERA model
Sample: Bacillus thuringiensis LexA repressor dimer, 47 kDa Bacillus thuringiensis protein
Bacteriophage pGIL01 gp7 tetramer, 24 kDa Bacteriophage pGIL01 protein
Buffer: 20 mM Hepes, 300 mM NaCl, 10% glycerol,, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-2000, University of British Columbia on 2017 Aug 25
Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor. Structure 27(7):1094-1102.e4 (2019)
Caveney NA, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka NCJ
RgGuinier 4.4 nm

SASDEE8 – Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), monomer from SEC-SAXS

UniProt ID: P32455 (1-592) farnesylated human Guanylate-binding protein 1
farnesylated human Guanylate-binding protein 1 experimental SAS data
Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), monomer from SEC-SAXS Rg histogram
Sample: Farnesylated human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 102 nm3

SASDEF8 – Human Guanylate Binding Protein 1 (hGBP1), monomer from SEC-SAXS

UniProt ID: P32455 (1-592) human Guanylate-binding protein 1
human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 (hGBP1), monomer from SEC-SAXS Rg histogram
Sample: Human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.9 nm
Dmax 13.4 nm
VolumePorod 106 nm3