SASDJQ6 – Full-length Collagenase H containing N-terminal Catalytic domain and C-terminal Non-Catalytic domains Polycystic Kidney disease domain 1 (PKD1), Polycystic Kidney disease domain 2 (PKD2) and Collagen Binding Domain (CBD)

MWexperimental 126 kDa MWexpected 112 kDa VPorod 198 nm3 log I(s) 3.83×101 3.83×100 3.83×10-1 3.83×10-2  s, nm-1 Log plot Log-Log plot

ln I(s) ln 3.83×101 Rg: 4.1 nm 0 (4.1 nm)-2 s2 (sRg)2I(s)/I(0) 1.104 0 √3 sRg p(r) Rg: 4.1 nm 0 Dmax: 14 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 0.004 4.289 Worse Better

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Synchrotron SAXS data from solutions of Full-length Collagenase H containing N-terminal Catalytic domain and C-terminal Non-Catalytic domains Polycystic Kidney disease domain 1 (PKD1), Polycystic Kidney disease domain 2 (PKD2) and Collagen Binding Domain (CBD) in 10 mM HEPES, 100 mM NaCl, 0.4 mM EGTA, 2.4 mM CaCl2, pH 7.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2 and 3 mg/ml were measured at 10°C. 50 successive 0.300 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve. Storage temperature = UNKNOWN

Collagenase ColH (Full-length) (ColH) Mol. type   Protein Organism   Hathewaya histolytica Olig. state   Monomer Mon. MW   112.0 kDa   UniProt   Q46085 (41-1021) Sequence   FASTA