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. 2019 May 24;9:73. doi: 10.1186/s13568-019-0795-4

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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.

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Fig. 1 — Purification and oligomerization behavior of a recombinant XylA from B. cenocepacia. a Size exclusion chromatogram obtained from Superdex 200 revealed a major peak. b Two major bands are observed on SDS-PAGE after size exclusion chromatography, revealing molecular sizes consistent with the monomer (ca. 54 kDa) and dimer (ca. 108 kDa) of His₆XylA fusion. c Native 4–20% gradient PAGE gel shows a single protein band of ca. 216 kDa, when all His₆XylA-containing fractions were pooled in a single sample. mAu, milli absorbance unit. *XylA containing fraction