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. Author manuscript; available in PMC: 2014 Jul 15.
Published in final edited form as: J Immunol. 2013 Jun 14;191(2):10.4049/jimmunol.1202014. doi: 10.4049/jimmunol.1202014

Table I.

Microscopy, image reconstruction, and modeling data

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 ----
a

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.

b

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).

c

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.

d

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.

e

Identification code of density map in EM Data Bank.

f

Protein Data Bank identification code for coordinate modeling results.

g

See Fig. S1 and Video 3. 80S particles were present in the 135S sample (cf. (15) and were used to compute the 80S-C3 reconstruction. More micrograph pairs were needed than were used for the 135S reconstruction because so few 80S particles were present per micrograph (see Fig. 2A).