Synchrotron SAXS data from solutions of aconitate hydratase B, monomer/dimer mixed fraction, in 100 mM NaCl, 20 mM Tris, 1 mM DTT, 3% v/v glycerol, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.70 mg/ml was measured at 20°C. 80 successive 0.100 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 molecular weight quoted is derived from concentration independent estimates spanning the credibility interval 127–162 kDa (expected MW of a full dimer is 192 kDa). Concentration dependent MW estimates, relative to a BSA standard, is estimated at approximately 113 kDa. Note - the data used to calculate the PDDF, and for model generation, was not normalised to protein concentration (ca. 4.7 mg/ml). The models displayed in this entry include: Top - a single GASBOR model representative of the dimer incorporating the volume fraction weighted monomer-dimer mixture fit to the data (35% volume fraction dimer, 65% volume fraction monomer) and; Bottom - the corresponding monomer and fit to the monomer-only data (estimated at 100% volume fraction monomer; and refer to SASBDB entry SASDND5). Alternative GASBORmx models are made available in the full entry zip archive (volume fractions are recorded in the header of the corresponding .pdb files).
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