SASDFR3 – Complex with 1H histone chaperone Vps75 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Asf1 (1H Vps75-H3:H4, 2H Rtt109-Asf1) acquired in 42% v/v D2O

MWexperimental 146 kDa MWexpected 145 kDa log I(s) 2.90×10-1 2.90×10-2 2.90×10-3 2.90×10-4  s, nm-1 Log plot Log-Log plot

ln I(s) ln 2.90×10-1 Rg: 3.1 nm 0 (3.1 nm)-2 s2 (sRg)2I(s)/I(0) 1.104 0 √3 sRg p(r) Rg: 3.2 nm 0 Dmax: 10.5 nm

Fits and models

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log I(s)  s, nm-1 Fit validation Metric Value pcormap χ² 0.000 4.964 Worse Better

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SANS data from solutions of the Asf1-H3:H4-Rtt109-Vps75 protein complex (1H Vps75-H3:H4, 2H Rtt109-Asf1) acquired in 42% v/v D2O in 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH 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 2 hrs 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 5.2 mg/mL, measured at 25°C. Number of frames = UNKNOWN

Vacuolar protein sorting-associated protein 75 (1-225 aa) (Vps75 1-225) Mol. type   Protein Organism   Saccharomyces cerevisiae Olig. state   Dimer Mon. MW   26.6 kDa   UniProt   P53853 (1-225) Sequence   FASTA   Histone acetyltransferase RTT109 (Rtt109) Mol. type   Protein Organism   Saccharomyces cerevisiae Olig. state   Monomer Mon. MW   50.1 kDa   UniProt   Q07794 (1-436) Sequence   FASTA   Histone chaperone ASF1 (Asf1) Mol. type   Protein Olig. state   Monomer Mon. MW   19.1 kDa   UniProt   P32447 (1-169) Sequence   FASTA   Histone H3.2 (35-135 aa) (H3 (35-135)) Mol. type   Protein Organism   Xenopus laevis Olig. state   Monomer Mon. MW   11.7 kDa   UniProt   P84233 (35-135) Sequence   FASTA   Histone H4 (H4) Mol. type   Protein Organism   Xenopus laevis Olig. state   Monomer Mon. MW   11.4 kDa   UniProt   P62799 (1-103) Sequence   FASTA   PDB ID   6O22