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. 2018 Nov 22;9:4943. doi: 10.1038/s41467-018-07129-6

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© The Author(s) 2018

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. 2 — Design and characterization of monomeric G3 fusion proteins and trimeric nanoassemblies. a Predicted structure of NanoLuc^TM luciferase (NL), superfolder green fluorescent protein (GFP), and chondroitinase ABC I (ChABC) monomeric G3 fusion proteins and trimeric nanoassemblies. b Approximate molecular weight determined under native conditions via size-exclusion chromatography. c Average hydrodynamic diameter estimated via dynamic light scattering. d Quantitative bioluminescence, fluorescence, and reaction velocity of NL, GFP, and ChABC fusions, respectively. PDB ID: 5IBO [10.2210/pdb5IBO/pdb] (NanoLuc^TM luciferase), 2B3P [10.2210/pdb2B3P/pdb] (superfolder GFP), 1HN0 [10.2210/pdb1HN0/pdb] (ChABC) for a. N ≥ 3, mean ± s.d. for c. N = 3, mean ± s.d. for d. Data for monomeric G3 fusion proteins appear as blue circles/traces, trimeric nanoassemblies as red triangles/traces