| 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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