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. 2016 Nov 30;72(Pt 12):892–896. doi: 10.1107/S2053230X16017921

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© Rouse et al. 2016

This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

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(a) Limited proteolysis of FapF. SDS–PAGE gel showing samples of FapF digested over a range of time periods with trypsin and chymotrypsin, with samples taken periodically over the course of 180 min as indicated (labelled in minutes). The protein is processed to produce stable fragments of approximately 35 or 31 kDa (indicated with arrows). Lane MW contains molecular-weight marker (labelled in kDa). (b) Purification of FapF. Superdex 200 (GE Healthcare) gel-filtration profile of FapF^106–430 in 0.5% C8E4. The main peak at 65 ml corresponds to FapF^106–430. Inset, SDS–PAGE of fractions from the FapF^106–430 nickel purification: M, marker; F, flowthrough; W1, first wash; W2, second wash; E, elution peaks 1 and 2.