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. 2016 Oct 13;6:126. doi: 10.3389/fcimb.2016.00126

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Copyright © 2016 Edgar, Chen, Kant, Rechkina, Rush, Forsberg, Jaehrig, Azadi, Tchesnokova, Sokurenko, Zhu, Korotkov, Pancholi and Korotkova.

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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Hemin binding induces SpyB oligomerization. (A) The size-exclusion chromatogram of MBP-SpyB monomer. (B) The size-exclusion chromatogram of MBP-SpyB monomer reconstituted with hemin in 1:4 ratio. (C) The size-exclusion chromatogram of MBP-SpyB monomer reconstituted with protoporphyrin IX in 1:4 ratio. The absorbance was monitored at 280 and 385 nm (hemin and protoporphyrin IX detection). (D) The appearance of WT MBP-SpyB, and double (C7A/C13A) and quadruple (C7A/C13A/C30A/C35A) MBP-SpyB mutants, following expression in E. coli Rosetta DE3 cells and purification by Ni-NTA affinity chromatography and size-exclusion chromatography. Data are representative of biological triplicates.