|
Synchrotron SAXS
data from solutions of
Candida glabrata Fructose Bisphosphate Aldolase (Fba1)
in
20 mM Tris-HCl pH, 300 mM NaCl, pH 8
were collected
on the
B21 beam line
at the Diamond Light Source storage ring
(Didcot, UK)
using a Eiger 4M detector
at a sample-detector distance of 3.7 m and
at a wavelength of λ = 0.09464 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 40.00 μl sample
at 1 mg/ml was injected at a 0.08 ml/min flow rate
onto a GE Superdex 200 Increase 10/300 column
at 15°C.
600 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.
Synchrotron SAXS data from solutions of Fructose-bisphosphate aldolase (Fba1) enzyme in 50 mM sodium phosphate, 500 mM NaCl, 500 mM imidazole, and 1 mM phenylmethylsulfonyl fluoride (PMSF) at pH 8.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.094 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 40.00 μl sample at 1 mg/ml was injected at a 0.07 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 15°C. 620 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.
|
|