| MWI(0) | 79 | kDa |
| MWexpected | 78 | kDa |
| VPorod | 121 | nm3 |
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log I(s)
6.34×10-3
6.34×10-4
6.34×10-5
6.34×10-6
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s, nm-1
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Unravelling the reaction mechanism of glutamate amidation in Staphylococcus aureus peptidoglycan
Francisco Miguel Piçarra Leisico, Mertens HD, PhD thesis, NOVA University Lisbon - (2022) URLSASDM22 – Staphylococcus aureus lipid II isoglutaminyl synthase MurT:GatD complex
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTLipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
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Fits and models
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Rg, nm
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Synchrotron SAXS data from solutions of S. aureus MurT:GatD complex in 100 mM Tris-HCl, 500 mM NaCl, 10 mM MgCl2, pH 8.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 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 4.1 mg/ml was injected at a 0.75 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 20°C. 1200 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.
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