Fig. 1: Cryo-EM structure of Redβ177 1-start helical assembly, resolved to 3.3 Å. | Nature Communications

Fig. 1: Cryo-EM structure of Redβ177 1-start helical assembly, resolved to 3.3 Å.

From: Redβ177 annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination

Fig. 1

a A representative electron micrograph displaying Redβ177 helices. Among the 4701 electron micrographs collected, all images identified as containing our protein sample displayed similar helical filaments. b A representative 2D class average of the helical filaments. c Fourier transform of a 2D class average. d Cryo-EM map of the 1-start helical assembly resolved to 3.3 Å. e Local resolution of the structure visible from both a side and a top view. f Plot showing the Fourier shell correlation (FSC) versus spatial frequency, for both the masked (red) and unmasked (blue) maps. The resolution of the structure was assessed using the point where the FSC curve crosses a correlation value of 0.143.

Back to article page