| MWexperimental | 47 | kDa |
| MWexpected | 48 | kDa |
| VPorod | 74 | nm3 |
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log I(s)
1.80×10-1
1.80×10-2
1.80×10-3
1.80×10-4
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s, nm-1
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High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M, Acta Crystallogr F Struct Biol Commun 76(Pt 9):414-421 (2020) Europe PMCSASDCK3 – Aldehyde dehydrogenase
Aldehyde-alcohol dehydrogenase|
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Fits and models
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Synchrotron SAXS data from solutions of aldehyde dehydrogenase in 30 mM HEPES, 150 mM NaCl, 5% (v/v) glycerol, pH 7.5 were collected on the B21 camera at the Diamond Light Source (Oxfordshire, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm ((Is) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 4°C. 18 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted to obtain the SAXS profile displayed in this entry.
Aldehyde dehydrogenase (AldDH) is the N-terminal domain of the bifunctional alcohol/aldehyde dehydrogenase (AdhE; SASBDB entry SASDC72) spanning amino acids 1-445 of the full-length protein. SAXS data were measured from a protein construct that included a C-terminal 6 x histidine affinity chromatography tag. The buffer subtraction was performed using Scatter. Subsequent analysis was performed using PRIMUS (ATSAS 2.7.1). |
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