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. 2012 Feb 2;5(4):515–521. doi: 10.1242/dmm.009324

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© 2012. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike License (http://creativecommons.org/licenses/by-nc-sa/3.0), which permits unrestricted non-commercial use, distribution and reproduction in any medium provided that the original work is properly cited and all further distributions of the work or adaptation are subject to the same Creative Commons License terms

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Fig. 2. — Regulation of OmpA localization by Stn. (A) SDS-PAGE of prepared protein fractions. Proteins were loaded on 10% gel in each lane as follows: 10 μg of whole cell protein fraction, 5 μg of secreted protein fraction, 10 μg of periplasmic protein fraction and 5 μg of total membrane protein fraction. Gel was stained with Coomassie Brilliant Blue R-250. M, protein marker; lane 1, wild type; lane 2, Δstn. (B,C) Transmission electron microscopic image of wild-type (B) and Δstn mutant (C) cells in ultrathin sections (magnification: 12,000×). Bacteria were cultured in LB medium at 37°C for 16 hours. (D–G) Immunogold labeling of OmpA using anti-OmpA antibody (magnification: 20,000×). Bacteria were cultured on LB agar plates at 37°C for 16 hours. D, wild-type strain; E, Δstn; F, ΔompA; G, wild type using normal mouse serum for control reaction. Arrows indicate the gold particles.