SASDFK7 – Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O

MWexperimental 145 kDa MWexpected 145 kDa log I(s) 2.00×10-2 2.00×10-3 2.00×10-4 2.00×10-5  s, nm-1 Log plot Log-Log plot

ln I(s) ln 2×10-2 Rg: 1.9 nm 0 (1.9 nm)-2 s2 (sRg)2I(s)/I(0) 1.104 0 √3 sRg p(r) Rg: 2.1 nm 0 Dmax: 5.5 nm

Fits and models

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log I(s)  s, nm-1 +3 Δ/σ -3  s, nm-1 Fit validation Metric Value pcormap χ² 0 0.696 Worse Better

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SANS data from solutions the Asf1-H3:H4-Rtt109-Vps75 protein complex (1H Asf1-H3(35-135):H4, bound to 70% 2H-labelled Rtt109-Vps75(1-225)) in 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pD 6.5 were collected on the D22 instrument at the ILL (Grenoble, France) using a 3He multidetector 128 linear sensitive Reuter-Stokes detector detector at a sample-detector/Collimation distance of 4 m/4 m and at a wavelength of λ = 0.6 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.55 mg/ml was measured at 25°C for 1 h. Storage temperature = 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