SASDJG9 – M100 DNA oligonucleotide bound to the protein fusion of Insulin gene enhancer protein Isl-1 LIM-interaction domain (Isl1-LID) and LIM/homeobox protein Lhx3 LIM-homeodomain (Lhx3-LIMHD): M100 + LLHD3

MWI(0) 41 kDa MWexpected 40 kDa VPorod 49 nm3 log I(s) 4.97×10-3 4.97×10-4 4.97×10-5 4.97×10-6  s, nm-1 Log plot Log-Log plot

ln I(s) ln 4.98×10-3 Rg: 3.6 nm 0 (3.6 nm)-2 s2 (sRg)2I(s)/I(0) 1.104 0 √3 sRg p(r) Rg: 3.9 nm 0 Dmax: 13 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 1.470 Worse Better

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log I(s)  s, nm-1 +3 Δ/σ -3  s, nm-1 Fit validation Metric Value pcormap χ² 0.197 1.468 Worse Better

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log I(s)  s, nm-1 +3 Δ/σ -3  s, nm-1 Fit validation Metric Value pcormap χ² 0.061 1.479 Worse Better

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Synchrotron SAXS data from solutions of LLHD3 (Isl1-LID fused to Lhx3-LIMHD) + M100 in 20 mM sodium phosphate buffer, 100 mM NaCl, 1 mM DTT, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 0.9 m and at a wavelength of λ = 0.108 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.12 mg/ml was measured at 27°C. 32 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. Storage temperature = UNKNOWN

M100 oligonucleotide (M100) Mol. type   DNA Olig. state   Monomer Mon. MW   12.4 kDa Sequence   FASTA   LIM/homeobox protein Lhx3 (Lhx3) Mol. type   Protein Organism   Mus musculus Olig. state   Monomer Mon. MW   23.2 kDa   UniProt   P50481 (28-227) Sequence   FASTA   Insulin gene enhancer protein ISL-1 (Isl1) Mol. type   Protein Organism   Mus musculus Olig. state   Monomer Mon. MW   4.2 kDa   UniProt   P61372 (262-291) Sequence   FASTA