| MWexperimental | 145 | kDa |
| MWexpected | 145 | kDa |
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log I(s)
3.10×10-1
3.10×10-2
3.10×10-3
3.10×10-4
|
s, nm-1
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Histone chaperone exploits intrinsic disorder to switch acetylation specificity.
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T, Nat Commun 10(1):3435 (2019) Europe PMCSASDFL3 – All 1H histone acetyltransferase Rtt109 complex with histones H3 and H4 and histone chaperones Asf1 and Vps75 (acquired in 100% v/v D2O)
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109
Histone chaperone ASF1
Histone H3.2 (35-135 aa)
Histone H4
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Fits and models
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SANS data from solutions of the all 1H Asf1-H3:H4-Rtt109-Vps75 protein complex in 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pD 6.5 were collected on the KWS1 instrument at FRM2 (Munich, Germany) using a SANS 6Li-Scintillator 1 mm thickness + photomultiplier detector. Data were collected at two sample detector positions: 1) 1.5 m for 1 hr using a neutron wavelength of 0.5 nm and; 2) 4 m for 2 hrs using a neutron wavelength of 0.5 nm. Both data sets were recorded on the same sample at 2.35 mg/mL, measured at 25°C.
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