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. Author manuscript; available in PMC: 2019 Dec 12.
Published in final edited form as: Nature. 2019 Jun 12;570(7761):338–343. doi: 10.1038/s41586-019-1295-z

Fig. 1 |. Biochemical characterization and cryo-EM structure determination.

Fig. 1 |

a, Schematic domain representation of human NLRP3 and NEK7, with labelled domain boundary defined from this work. b, MST analysis of NEK7 binding to NLRP3. A dissociation constant of 78.9 ± 38.5 nM was calculated from three independent replicates (shown as mean ± s.d.). c, Reconstitution of NLRP3-NEK7 dimer and monomer complexes on Superdex 200 gel filtration column (repeated ≥ 5 times). Molecular mass distribution within each peak was calculated from in-line MALS measurements, and shown in blue and orange for the dimer and monomer complexes, respectively (Performed once). d, SDS-PAGE gels of eluted fractions of dimer and monomer complexes (repeated ≥ 5 times). e, Representative 2D class averages from the 300 keV cryo-EM dataset, selected amongst 100 classes. f, The final cryo-EM density map (shown at 6σ) in three orientations and coloured with local resolutions by ResMap48.