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. 2022 Aug 29;13:967949. doi: 10.3389/fmicb.2022.967949

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Copyright © 2022 Chai, Whittall, Polyak, Foo, Li, Dutschke, Ogunniyi, Ma, Sykes, Semple and Venter.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Purification of AbFtsZ AbFtsZ was cloned in the pET-41a(+) vector and expressed in BL21(DE3) E. coli via induction with 1 mM IPTG. The protein was purified from the cytoplasmic fraction using Nickel-affinity column chromatography. The different fractions from the purification process were loaded onto SDS-PAGE (4–12%). Protein was visualized by staining with Coomassie^® Brilliant Blue R-250. Purified AbFtsZ (43.4 kDa) is observed as indicated by the arrow. The protein concentration was determined using the standard Bio-Rad™ BCA Protein Assay Kit.