UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109
UniProt ID: P32447 (1-169) Histone chaperone ASF1
UniProt ID: P62799 (1-103) Histone H4
UniProt ID: Q6PI79 (1-136) Histone H3 full-length
UniProt ID: P53853 (1-264) Vacuolar protein sorting-associated protein 75 full-length
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Sample: |
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein
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Buffer: |
50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5 |
Experiment: |
SANS
data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9
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Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections)
Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
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RgGuinier |
3.1 |
nm |
Dmax |
9.5 |
nm |
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