TABLE 1.
AiV-1 virion and empty particle structure quality indicators
| Parameter | AiV-1 empty particle cryo-EM structure | AiV-1 virion crystal structureb |
|---|---|---|
| Space group | NAd | I23 |
| Unit cell dimensions | ||
| a, b, c (Å) | NA | 350.80, 350.80, 350.80 |
| α, β, γ (°) | NA | 90, 90, 90 |
| Resolution (Å) | 4.2 | 72.0–2.3 (2.34–2.30) |
| Rmergea | NA | 0.15 (0.63) |
| 〈I〉/〈σI〉 | NA | 6.0 (1.8) |
| Completeness (%) | NA | 91.0 (94.0) |
| Observation multiplicity | NA | 3.2 (3.0) |
| No. of observations | NA | 902,384 (43,198) |
| No. of unique observations | NA | 282,853 (14,471) |
| Rwork | 0.34 | 0.33e |
| No. of: | ||
| Protein atoms* | 5,455 | 5,791 |
| Water atoms* | NA | 147 |
| RMSD | ||
| Bond lengths (Å) | 0.016 | 0.013 |
| Bond angles (°) | 1.57 | 1.43 |
| Ramachandran statistics (%)c | ||
| Preferred regions | 89.1 | 95.7 |
| Allowed regions | 8.4 | 4.0 |
| Disallowed regions | 2.5 | 0.3 |
| Avg atomic B factor (Å2) | 127.8 | 22.9 |
a
Rmerge = ΣhΣj|lhj − 〈lh〉|/ΣΣ|lhj|. *, Statistics are given for one icosahedral asymmetric unit.
b
Statistics for the highest-resolution shell are indicated in parentheses.
c
Determined according to the criterion of Molprobity (78).
d
NA, not applicable.
e
All reflections were used in the refinement. The Rfree value, if it were calculated, would be very similar to Rwork because of the 5-fold noncrystallographic symmetry present in the crystal. Therefore, the Rfree would not provide an unbiased measure of model quality in this case (55).