Table 1.
Parameters of three-dimensional reconstructions of myosin configurations
| Myosin (state) | No. of reconstructions (micrographs) | No. of actomyosin molecules | Mean phase residual (degrees) |
|---|---|---|---|
| S329E (rigor) | 26 (5) | 4,752 | 28 (20–40) |
| S329A (rigor) | 22 (4) | 3,402 | 30 (20–44) |
| S329E (Mg-ADP) | 25 (6) | 4,536 | 36 (21–43) |
Each density map combined the stated number of individual reconstructions (usually two reconstructions per filament, corresponding to the near and far sides) from the stated number of micrographs, which together contained the stated number of actomyosin molecules. The internal consistency of each data set is expressed in terms of the mean phase residual over all strong layer lines out to an axial spacing of 24 Å−1, averaged over the full data set. The numbers in parentheses give the range of this residual for individual filaments in the data set.