| MWexperimental | 318 | kDa |
| MWexpected | 229 | kDa |
| VPorod | 546 | nm3 |
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log I(s)
1.28×10-1
1.28×10-2
1.28×10-3
1.28×10-4
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s, nm-1
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BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function.
Grinter R, Morris FC, Dunstan RA, Leung PM, Kropp A, Belousoff M, Gunasinghe SD, Scott NE, Beckham S, Peleg AY, Greening C, Li J, Heinz E, Lithgow T, mBio :e0148021 (2021) Europe PMCSASDJW3 – YraP from Acinetobacter baumannii full-length, minus signal-peptide and acyl anchoring cysteine
BON domain protein|
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Fits and models
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Synchrotron SAXS data from solutions of YraP from Acinetobacter baumannii in 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH 7.8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.10322 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 50.00 μl sample at 10.5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 20 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.
SEC-SAXS analysis of the YraP protein from Acinetobacter baumannii, with the signal peptide and acyl-chain modified cysteine removed. In the cell, the protein has been experimentally shown to localize to the outer membrane. In solution, the protein has been shown to adopt a decameric oligomerization state. |
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