| MWI(0) | 83 | kDa |
| MWexpected | 81 | kDa |
| VPorod | 126 | nm3 |
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log I(s)
2.59×10-2
2.59×10-3
2.59×10-4
2.59×10-5
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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) URLSASDLZ9 – Streptococcus pneumoniae lipid II isoglutaminyl synthase MurT:GatD complex (no Zn2+)
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. pneumoniae MurT:GatD complex in 50 mM Hepes, 10 mM MgCl2, 500 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 55.00 μl sample at 6.5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 900 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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