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. 2019 Jun 24;14(6):e0218474. doi: 10.1371/journal.pone.0218474

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© 2019 Holtrup et al

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

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Fig 6 — (A) Evaluation of aggregation and 2-D crystalline protein assembly of recombinant Strep-HP1542 in low spin-down assays (left panels) and with electron microscopy (right panels) after various treatments. Conditions were indicated. (B) Upper panel: Spin-down assay of HP1542_1-339 after purification from E. coli. Pictogram is demonstrating the procedure. Samples were split in two equal fractions: the upper one was defined as soluble fraction (S) and the remaining one was defined as gel-like-pellet fraction (P). Lower panel: transmission electron microscope (TEM) images of purified HP1542_1-339 in low (and higher magnification (inlet)) Scale bars 100 nm.