UniProt ID: (None-None) 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)
UniProt ID: P06897 (None-None) Histone H2A type 1
UniProt ID: P02281 (None-None) Histone H2B 1.1
UniProt ID: P84233 (1-136) Histone H3.2
UniProt ID: P62799 (None-None) Histone H4
|
|
|
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 |
|
|
UniProt ID: P32657 (118-1274) Chromodomain-helicase-DNA-binding protein 1
UniProt ID: (None-None) 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)
UniProt ID: P06897 (None-None) Histone H2A type 1
UniProt ID: P02281 (None-None) Histone H2B 1.1
UniProt ID: P84233 (1-136) Histone H3.2
UniProt ID: P62799 (None-None) Histone H4
|
|
|
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 |
|
|
UniProt ID: P32657 (118-1274) Chromodomain-helicase-DNA-binding protein 1
UniProt ID: (None-None) 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)
UniProt ID: P06897 (None-None) Histone H2A type 1
UniProt ID: P02281 (None-None) Histone H2B 1.1
UniProt ID: P84233 (1-136) Histone H3.2
UniProt ID: P62799 (None-None) Histone H4
|
|
|
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 |
|
|
UniProt ID: P32657 (118-1274) Chromodomain-helicase-DNA-binding protein 1
UniProt ID: (None-None) 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)
UniProt ID: P06897 (None-None) Histone H2A type 1
UniProt ID: P02281 (None-None) Histone H2B 1.1
UniProt ID: P84233 (1-136) Histone H3.2
UniProt ID: P62799 (None-None) Histone H4
|
|
|
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 |
|
|
UniProt ID: Q92133 (None-None) Histone H3
UniProt ID: P62799 (None-None) Histone H4
UniProt ID: P06897 (None-None) Histone H2A type 1
UniProt ID: Q92130 (None-None) Histone H2B
UniProt ID: None (None-None) Non-linker Ended Trinucleosome DNA
|
|
|
Sample: |
Histone H3 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B monomer, 14 kDa Xenopus laevis protein
Non-linker Ended Trinucleosome DNA monomer, 172 kDa DNA
|
Buffer: |
20 mM Tris 150 mM NaCl 1 mM EDTA 1 mM DTT 50% w/v sucrose, pH: 7.5 |
Experiment: |
SAXS
data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Mar 11
|
Solution structure(s) of trinucleosomes from contrast variation SAXS
Nucleic Acids Research (2021)
Mauney A, Muthurajan U, Luger K, Pollack L
|
RgGuinier |
12.9 |
nm |
Dmax |
41.8 |
nm |
|
|