| MWexperimental | 25 | kDa |
| MWexpected | 30 | kDa |
| VPorod | 34 | nm3 |
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log I(s)
3.83×10-3
3.83×10-4
3.83×10-5
3.83×10-6
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s, nm-1
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Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains
Ariza A, Liu Q, Cowieson N, Ahel I, Filippov D, Rack J, Journal of Biological Chemistry :107770 (2024) DOISASDTY8 – Streptococcus pyogenes Protein-ADP-ribose hydrolase
Protein-ADP-ribose hydrolase (D13G, Y23S, T61A, I114S, R177H, I246T)|
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Fits and models
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Synchrotron SAXS data from solutions of Streptococcus pyogenes Protein-ADP-ribose hydrolase in 50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT, 5% (v/v) glycerol, pH 8 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 6 mg/ml was injected at a 0.16 ml/min flow rate onto a Shodex KW403-4F column at 15°C. 600 successive 3 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.
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