MACROMOLECULE TYPE: heterocomplex

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

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

SASDEH3 – TubR protein of the pXO1-like plasmid pBc10987 from B. cereus (Bc-TubR) bound to S48 DNA (Bc-TubR : S48 DNA complex)

S48 DNA strand 1S48 DNA strand 2TubR of the pXO1-like plasmid pBc10987 from B. cereus (Bc-TubR) experimental SAS data
MOLECULAR DYNAMICS FRAME model
Sample: S48 DNA strand 1 monomer, 21 kDa DNA
S48 DNA strand 2 monomer, 21 kDa DNA
TubR of the pXO1-like plasmid pBc10987 from B. cereus (Bc-TubR) decamer, 137 kDa protein
Buffer: 0.1 M NaCl, 10 mM Tris, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Nov 28
Cooperative DNA Binding of the Plasmid Partitioning Protein TubR from the Bacillus cereus pXO1 Plasmid. J Mol Biol (2018)
Hayashi I, Oda T, Sato M, Fuchigami S
RgGuinier 6.1 nm
Dmax 23.0 nm
VolumePorod 305 nm3

SASDJX2 – Modification dependent EcoKMcrA restriction endonuclease in complex with cognate hemimethylated 12bp oligoduplex

cognate hemimethylated 12-bp oligoduplex5-methylcytosine-specific restriction enzyme A experimental SAS data
SASREF model
Sample: Cognate hemimethylated 12-bp oligoduplex dimer, 15 kDa DNA
5-methylcytosine-specific restriction enzyme A dimer, 65 kDa Escherichia coli protein
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 3.9 nm
Dmax 13.5 nm
VolumePorod 69 nm3

SASDJZ2 – N-terminal domain of modification dependent EcoKMcrA restriction endonuclease in complex with cognate hemimethylated 12bp oligoduplex

5-methylcytosine-specific restriction enzyme A (N-terminal domain)cognate hemimethylated 12-bp oligoduplex experimental SAS data
OTHER model
Sample: 5-methylcytosine-specific restriction enzyme A (N-terminal domain) monomer, 21 kDa Escherichia coli protein
Cognate hemimethylated 12-bp oligoduplex monomer, 7 kDa DNA
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 29 nm3

SASDDU8 – Multidomain architecture of the estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains

Estrogen receptorERE1ERE2EstradiolhERa peptide1hERa peptide2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Estrogen receptor dimer, 85 kDa protein
ERE1 monomer, 6 kDa Homo sapiens DNA
ERE2 monomer, 6 kDa Homo sapiens DNA
Estradiol dimer, 0 kDa
HERa peptide1 monomer, 2 kDa protein
HERa peptide2 monomer, 2 kDa protein
Buffer: 10 mM CHES (pH9.5), 125 mM NaCl, 5mM KCl, 4 mM MgCl2, 50 mM arginine, 50 mM glutamate, 5 mM TCEP, 5% glycerol, 10 µm Zn acetate, 10 µM estradiol, pH: 9.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Aug 10
Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains. Nat Commun 9(1):3520 (2018)
Huang W, Peng Y, Kiselar J, Zhao X, Albaqami A, Mendez D, Chen Y, Chakravarthy S, Gupta S, Ralston C, Kao HY, Chance MR, Yang S
RgGuinier 3.8 nm
Dmax 11.5 nm

SASDCT6 – 12N12 nucleosome in 60% sucrose with ADP-BeF3

169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data
12N12 nucleosome in 60% sucrose with ADP-BeF3 Rg histogram
Sample: 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein
Histone H3.2 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2), pH: 7.8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24
The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
RgGuinier 4.8 nm
Dmax 14.0 nm

SASDCU6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose without any nucleotides added (Apo)

Chromodomain-helicase-DNA-binding protein 1169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data
Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose without any nucleotides added (Apo) Rg histogram
Sample: Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein
169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein
Histone H3.2 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, pH: 7.8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24
The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
RgGuinier 5.2 nm
Dmax 12.8 nm

SASDCV6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3

Chromodomain-helicase-DNA-binding protein 1169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data
Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3 Rg histogram
Sample: Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein
169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein
Histone H3.2 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2), pH: 7.8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24
The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
RgGuinier 5.3 nm
Dmax 16.5 nm

SASDCW6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with AMP-PNP

Chromodomain-helicase-DNA-binding protein 1169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data
Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with AMP-PNP Rg histogram
Sample: Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein
169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein
Histone H3.2 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, 0.5 mM AMP-PNP, pH: 7.8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24
The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
RgGuinier 5.6 nm
Dmax 16.7 nm

SASDDT5 – Ribonucleoprotein complex of nonstructural protein sigma NS bound to 20mer RNA (NS-RNP20)

Nonstructural protein sigma NS20mer RNA (unstructured) experimental SAS data
Nonstructural protein sigma NS 20mer RNA (unstructured) Kratky plot
Sample: Nonstructural protein sigma NS octamer, 325 kDa Avian orthoreovirus protein
20mer RNA (unstructured) dimer, 13 kDa RNA
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Feb 25
Stability of local secondary structure determines selectivity of viral RNA chaperones. Nucleic Acids Res (2018)
Bravo JPK, Borodavka A, Barth A, Calabrese AN, Mojzes P, Cockburn JJB, Lamb DC, Tuma R
RgGuinier 7.8 nm
Dmax 38.0 nm
VolumePorod 964 nm3