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. 2019 Jul 26;19:169. doi: 10.1186/s12866-019-1544-1

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© The Author(s). 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 3 — Column-bound YpeB_∆25–203 K437C cross-linked complex. Two hundred optical density units of decoated dormant spores were cross-linked with APB. Cross-linked spores were lyophilized and mechanically broken. Proteins were extracted with 8 M urea binding buffer for 2 h. Spore lysates (lanes 2–3) were then passed over a Ni²⁺ NTA column to isolate YpeB_∆25–203-His₆ in addition to those proteins covalently bound via cross-links. Flow-thru (lanes 4–5) and bound (lanes 6–7) fractions were visualized via western blot using anti-YpeB antibodies [20]. The positions of protein size markers (lane 1) are indicated on the left. YpeB∆25–203 K437C monomers and dimers were detected in both the load (lane 3) and bound (lane 7) fractions of cross-linked spore samples