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- W2991070391 abstract "The membrane protein EsaA is a conserved component of the type VIIb secretion system. Limited proteolysis of purified EsaA from Staphylococcus aureus USA300 identified a stable 48 kDa fragment, which was mapped by fingerprint mass spectrometry to an uncharacterized extracellular segment of EsaA. Analysis by circular dichroism spectroscopy showed that this fragment folds into a single stable domain made of mostly α-helices with a melting point of 34.5°C. Size-exclusion chromatography combined with multi-angle light scattering indicated the formation of a dimer of the purified extracellular domain. Octahedral crystals were grown in 0.2 M ammonium citrate tribasic pH 7.0, 16% PEG 3350 using the hanging-drop vapor-diffusion method. Diffraction data were analyzed to 4.0 Å resolution, showing that the crystals belonged to the enantiomorphic tetragonal space groups P 4 1 2 1 2 or P 4 3 2 1 2, with unit-cell parameters a = 197.5, b = 197.5, c = 368.3 Å, α = β = γ = 90°." @default.
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- W2991070391 date "2019-11-20" @default.
- W2991070391 modified "2023-09-27" @default.
- W2991070391 title "An extracellular domain of the EsaA membrane component of the type VIIb secretion system: expression, purification and crystallization" @default.
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- W2991070391 doi "https://doi.org/10.1107/s2053230x1901495x" @default.
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