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. Author manuscript; available in PMC: 2012 Sep 1.
Published in final edited form as: J Struct Biol. 2011 May 17;175(3):384–393. doi: 10.1016/j.jsb.2011.05.012

Figure 5.

Figure 5

(A) A full CCD frame of ε15 bacteriophage at ~70,000× detector magnification at ~0.6 μm under-focus. (B) The central portion of the Fourier transform of the image in A. The boundaries of the box correspond to 1/2 Nyquist. The right half has been processed to better visualize the Thon rings. (C) The rotationally-averaged power spectrum (left axis) and spectral SNR (right axis) from the Fourier transform in B. (D) The icosahedral 3D reconstruction, with the 3-fold symmetry axis in the middle of the image shown. (E) The Fourier shell correlation (FSC) between reconstructions of two half data sets reveals the final resolution is 7.2 Å (0.35 Nyquist) by 0.5 FSC or 5.7 Å (0.45 Nyquist) by 0.143 FSC. (F) A view of the 3-fold symmetry axis from the inside of the capsid. Secondary structure is clearly distinguishable, including the long α-helix in the zoomed view.