Fig. 7: Insertion of mRuby2 within the central domain of PbINP.
From: Water-organizing motif continuity is critical for potent ice nucleation protein activity
a An illustration of the R9-mRuby2-PbINP construct, where the large fluorescent protein replaces repeats 8 to 27. Domain colors are identical to those in Fig. 2. Known and modeled structures are presented in ribbon format. The red curved arrow depicts the re-positioning of mRuby2 towards the C terminus by twelve repeats in R21-mRuby2-PbINP. b Representative fluorescence microscopy images (n = 3, scale bar: 10 µm) of post-induction E. coli producing the R9-mRuby2-PbINP. The left and right panels were obtained after excitation at 488 and 560 nm, respectively. The middle panel is an overlay of these two images. c WISDOM and BINARY T50 values for R9- and R21-mRuby2-PbINP, as well as the 33-repeat, 46-repeat, and full-length (65-repeat) constructs. The temperature uncertainty for both the WISDOM and BINARY experiments is ±0.3 °C.
