| MWexperimental | 16 | kDa |
| MWexpected | 28 | kDa |
| VPorod | 41 | nm3 |
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log I(s)
3.23×10-3
3.23×10-4
3.23×10-5
3.23×10-6
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s, nm-1
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Similar but Distinct—Biochemical Characterization of the
Staphylococcus aureus
Serine Hydrolases FphH
and FphI
Fellner M,
Randall G,
Bitac I,
Warrender A,
Sethi A,
Jelinek R,
Kass I,
Proteins: Structure, Function, and Bioinformatics
(2024)
DOISASDV64 – Serine hydrolase FphH with short chain esterase activity (Apo FphH)
Alpha/beta fold hydrolase|
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Fits and models
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Synchrotron SAXS data from solutions of Apo FphH in 100 mM NaCl, 10 mM HEPES, pH 7.6 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.5 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 40.00 μl sample at 5.4 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column at 21°C. 16 successive 0.500 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.
A serine hydrolase with short chain esterase activity, active in biofilm life cycle of S. aureus. Two shape reconstructions are displayed: 1) DAMFILT (top) derived from the volume and bead occupancy corrected spatial alignment of several individual DAMMIF models and; 2) An individual DAMMIF model example (bottom) with the corresponding fit to the data shown to the left. |
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