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. Author manuscript; available in PMC: 2017 Jan 5.
Published in final edited form as: Structure. 2015 Dec 24;24(1):37–42. doi: 10.1016/j.str.2015.11.009

Figure 1. Cryo-EM analysis reveals co-existence of PhnG2H2I2J2 and PhnG2H2I2J2K.

Figure 1

(A) The series of the enzymatic steps of C-P lyase. (B) A region of a representative micrograph showing the particles of PhnG2H2I2J2 and PhnG2H2I2J2K with a defocus of - 1.2 μm. The scale bar denotes 500Å. (C) Power spectrum of the same micrograph in (B). The white dashed curve shows the Nyquist at 3Å. (D) 3D density maps of PhnG2H2I2J2 (left) and PhnG2H2I2J2K (right). The maps were colored based on the local resolutions. (E) Projections of the two maps compared to the reference-free class averages in two representative orientations. The Euler angles were based on the EMAN2 convention. Yellow arrows indicate the location of PhnK. See also Figure S1.