SASBDB entries for UniProt ID:

SASDAZ6 – CyaY-dimer and IscS-dimer complex

UniProt ID: P0A6B7 (None-None) Cysteine desulfurase IscS

UniProt ID: P27838 (None-None) Protein CyaY
Cysteine desulfurase IscSProtein CyaY experimental SAS data
SASREF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 10 mM β-mercaptoethanol and ferrous ammonium sulphate, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.1 nm
Dmax 10.9 nm

SASDA27 – IcsS, IscU and CyaY dimeric complex

UniProt ID: P0A6B7 (None-None) Cysteine desulfurase IscS

UniProt ID: P0ACD4 (None-None) Iron-sulfur cluster assembly scaffold protein IscU

UniProt ID: P27838 (None-None) Protein CyaY
Cysteine desulfurase IscSIron-sulfur cluster assembly scaffold protein IscUProtein CyaY experimental SAS data
SASREF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Iron-sulfur cluster assembly scaffold protein IscU dimer, 29 kDa Escherichia coli protein
Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.5 nm
Dmax 11.9 nm

SASDA37 – Surface Protein G (SasG) EG5 repeat protein G51-G52

UniProt ID: Q2G2B2 (420-629) Surface protein G
Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 24 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 4.7 nm
Dmax 19.0 nm
VolumePorod 29 nm3

SASDA47 – Surface Protein G (SasG) EG5 repeat protein G51-G53

UniProt ID: Q2G2B2 (419-757) Surface protein G
Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 39 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 7.7 nm
Dmax 30.5 nm
VolumePorod 49 nm3

SASDA57 – Surface Protein G (SasG) EG5 repeat protein G51-G54

UniProt ID: Q2G2B2 (419-885) Surface protein G
Surface protein G experimental SAS data
GASBOR model
Sample: Surface protein G monomer, 53 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 9.7 nm
Dmax 38.5 nm
VolumePorod 58 nm3

SASDA67 – Surface Protein G (SasG) EG5 repeat protein G51-G55

UniProt ID: Q2G2B2 (419-1013) Surface protein G
Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 67 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 12.0 nm
Dmax 48.0 nm
VolumePorod 87 nm3

SASDA77 – Surface Protein G (SasG) EG5 repeat protein G51-G56

UniProt ID: Q2G2B2 (419-1141) Surface protein G
Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 81 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 14.1 nm
Dmax 57.0 nm
VolumePorod 89 nm3

SASDA87 – Surface Protein G (SasG) EG5 repeat protein G51-G57

UniProt ID: Q2G2B2 (419-1269) Surface protein G
Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 95 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 15.9 nm
Dmax 63.0 nm
VolumePorod 122 nm3

SASDAA7 – Heterotetramer of histidine protein kinase and response regulator

UniProt ID: Q8DMW4 (216-441) Histidine protein kinase

UniProt ID: Q8DMW5 (1-250) Response regulator
Histidine protein kinaseResponse regulator experimental SAS data
BUNCH model
Sample: Histidine protein kinase dimer, 54 kDa Streptococcus pneumoniae protein
Response regulator dimer, 61 kDa Streptococcus pneumoniae protein
Buffer: 20 mM Tris 200 mM NaCl 5% (v/v) Glycerol 5 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, IBBMC on 2012 May 16
Modeling the ComD/ComE/comcde interaction network using small angle X-ray scattering. FEBS J 282(8):1538-53 (2015)
Sanchez D, Boudes M, van Tilbeurgh H, Durand D, Quevillon-Cheruel S
RgGuinier 4.0 nm
Dmax 16.0 nm
VolumePorod 175 nm3

SASDAB7 – Complex ComE-comcde

UniProt ID: (None-None) comcde

UniProt ID: Q8DMW5 (1-250) Response regulator
comcdeResponse regulator experimental SAS data
OTHER model
Sample: Comcde, 24 kDa Streptococcus pneumoniae DNA
Response regulator dimer, 61 kDa Streptococcus pneumoniae protein
Buffer: 50 mM MES 500 mM NaCl 5% (v/v) Glycerol 5 mM β-mercaptoethanol, pH: 6.2
Experiment: SAXS data collected at SWING, SOLEIL on 2011 Feb 11
Modeling the ComD/ComE/comcde interaction network using small angle X-ray scattering. FEBS J 282(8):1538-53 (2015)
Sanchez D, Boudes M, van Tilbeurgh H, Durand D, Quevillon-Cheruel S
RgGuinier 3.4 nm
Dmax 10.7 nm
VolumePorod 122 nm3