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. 2016 Nov 9;7:1802. doi: 10.3389/fmicb.2016.01802

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Copyright © 2016 Dahlin, Srivastava, Bulone and McKee.

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) or licensor 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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SDS-PAGE analysis and identity confirmation of the recombinant SpLASA protein. (A) The recombinant protein expressed in E. coli was purified by immobilized metal ion affinity chromatography (IMAC). (B) The identity of the Coomassie blue-stained SDS-PAGE band was confirmed by mass spectrometry analysis after in-gel partial proteolysis with trypsin. The peptides identified unequivocally confirmed that the purified recombinant protein corresponds to SpLASA. The corresponding spectra are presented in Supplementary Figure S2.