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. 2020 Jan 13;11:239. doi: 10.1038/s41467-019-13897-6

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Dimerization interface in RpBphP2-derived iRFPs. The residues substituted based on alignment with RpBphP1-derived miRFPs are in yellow. The BV chromophore is in blue. The model is based on RpBphP2-PAS-GAF structure (PDB ID: 4R6L). b Alignment of C-termini from parental BphPs, i.e. RpBphP1, RpBphP2 and RpBphP6, monomeric RpBphP1-derived miRFPs, and monomerized iRFPs of RpBphP2 and RpBphP6 origins. The substituted residues are marked in yellow. c Fusions of miRFP713 (representative monomerized iRFP derived from RpBphP2) and miRFP670–2 (representative monomerized iRFP derived from RpBphP6) labeling actin (LifeAct) and tubulin in live HeLa cells. Scale bar, 10 µm. d Brightness of monomerized iRFPs in comparison with dimeric iRFPs and previously reported monomeric NIR FPs. Columns are highlighted according to the origin of NIR FPs (RpBphP2-derived FPs in red, RpBphP6-derived in green and RpBphP1-derived in cyan) and their oligomeric state (dimeric are dashed, monomeric are plain). Error bars are double s.e.m. (n = 3; transfection experiments).