| MWexperimental | 145 | kDa |
| MWexpected | 145 | kDa |
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log I(s)
1.70×10-2
1.70×10-3
1.70×10-4
1.70×10-5
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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 PMCSASDFM3 – Complex with 1H histone chaperone Asf1 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1H Asf1-H3:H4, 2H Rtt109-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 Asf1-H3:H4-Rtt109-Vps75 protein complex (protonated Asf1-H3:H4 bound to perdeuterated Rtt109-Vps75) 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. Due to a combination of negative (from 1H Asf1-H3:H4) and positive (from perdeuterated Rtt109-Vps75) contrasts the Rg obtained from the Guinier approximation is negative. The data were recorded at two detector configurations: 1) 4 m for 6 hrs using a neutron wavelength of 0.5 nm and; 2) 1.5 m for 2.5 hrs using a neutron wavelength of 0.5 nm. Both measurement were performed on the same sample at 3.85 mg/mL, measured at 25°C.
Number of frames = UNKNOWN |
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