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. 2007 Aug;65(4):1106–1121. doi: 10.1111/j.1365-2958.2007.05851.x

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© 2007 The Authors; Journal compilation © 2007 Blackwell Publishing Ltd

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Fig. 5 — Immunoblotting (IB) analysis of the protein complex with anti-MurG, anti-MreB and anti-β-lactamase under non-reducing conditions. The membranes extracted from BW25113ΔmraY/pMAKmraYec strain (MraY–β-lactamase–His expressing strain) were used for the IP (with cross-linking) with anti-MurG. The blot was then probed with anti-MurG (lanes 1 and 2), anti-MreB (lanes 3 and 4) or anti β-lactamase (lanes 5 and 6). In parallel the same IP was performed without the membrane fraction (lanes 1, 3 and 5). A cross-linked product with a molecular weight of about 120 kDa is visible in all samples except in control samples (lanes 1, 3 and 5). The faint band in lane 2 is MurG, which is not completely cross-linked in the protein complex. The band in lane 6 with the molecular weight of approximately 70 kDa corresponds to the MraY–β-lactamase–His protein that is not completely cross-linked in the protein complex.