| MWexperimental | 186 | kDa |
| MWexpected | 214 | kDa |
| VPorod | 390 | nm3 |
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log I(s)
1.36×102
1.36×101
1.36×100
1.36×10-1
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s, nm-1
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Kinetic and Structural Characterization of a Flavin-Dependent Putrescine N-Hydroxylase from Acinetobacter baumannii.
Lyons NS, Bogner AN, Tanner JJ, Sobrado P, Biochemistry (2022) Europe PMCSASDNB9 – Acinetobacter baumannii putrescine N-hydroxylase, 3 mg/mL
L-lysine 6-monooxygenase (NADPH-requiring)|
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Fits and models
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Synchrotron SAXS
data from solutions of
Acinetobacter baumannii putrescine N-hydroxylase, 3 mg/mL
in
25 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP, 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 2 m and
at a wavelength of λ = 0.1234 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 3.00 mg/ml was measured
at 20°C.
30 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 deposited scattering curve was averaged using FrameSlice, using frames 1-2 in the Guinier region and frames 1-30 in the other q regions. The first 6 (lowest q) data points were omitted based on analysis with Primus AutoRg. |
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