Table I.
Sample | Micrograph focal pairsa |
Pixel size (Å) |
Particle imagesb |
CTF correctionc |
Resolu tiond (Å) |
EMDB IDe |
PDB IDf |
---|---|---|---|---|---|---|---|
160S-C3 | 6 | 1.82 | 4184 | full | 11.1 | 5291 | 3J3O |
135S-C3 | 2 | 1.84 | 9810 | full | 9.1 | 5292 | 3J3P |
80S-C3g | 7 | 1.84 | 238 | phases only | 22 | 5293 | ---- |
Pairs of micrographs taken of the same field-of-view and used to compute 3D reconstructions, first image taken closer-to-focus, second image farther-from-focus. The 135S-C3 micrographs contained many more particles per micrograph than did micrographs of 160S-C3 complexes. Therefore, only two micrograph pairs were needed to compute the 135S-C3 structure.
Total number of particle images extracted from micrographs and used to compute the 3D reconstruction, divide by two for the number of image pairs (focal pairs).
Correction for the final, published reconstruction: full, deconvolution of CTF and correction for decay (see Materials and Methods); or, phases-only, corrected only for the phase-flipping effects of the CTF.
Data set split in two, reconstructions computed and compared via Fourier shell correlation. Resolution determined by the point at which the Fourier shell correlation value reaches 0.5, for reconstructions computed from images that were only corrected for phase-flipping of the CTF.
Identification code of density map in EM Data Bank.
Protein Data Bank identification code for coordinate modeling results.