Table 1. Data collection and refinement statistics (molecular replacement).
| NavMs wild type (5HVX) | NavMs I218C (5HVD) | |
|---|---|---|
| Data collection | ||
| Space group | I422 | I422 |
| Cell dimensions | ||
| a, b, c (Å) | 109.0, 109.0, 210.6 | 109.6 109.6 209.7 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0 90.0 90.0 |
| Resolution (Å) | 48.4–2.4 (2.55–2.45)* | 58.6–2.6 (2.72–2.60) |
| Rmerge | 0.30 (2.58) | 0.29 (3.60) |
| Rpim | 0.06 (0.49) | 0.045 (0.095) |
| I/σ(I) | 16.5 (1.4) | 15.8 (1.4) |
| CC1/2 | 1.00 (0.77) | 0.99 (0.70) |
| Completeness(%) | 100.0 (100.0) | 100.0 (99.7) |
| Redundancy | 28.2 (29.3) | 43.3 (45.5) |
| Refinement | ||
| Resolution (Å) | 27.7–2.45 | 26.57–2.60 |
| No. of reflections | 670,458 | 868,621 |
| Rwork/Rfree | 0.209/0.238 | 0.200/0.228 |
| No. of atoms | ||
| Protein | 1,980 | 1,976 |
| Ligand/ion | 85 | 69 |
| Water | 100 | 111 |
| B factors | ||
| Protein | 98.9 | 93.4 |
| Ligand/ion | 120.8 | 104.0 |
| Water | 93.9 | 86.0 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.010 | 0.010 |
| Bond angles (°) | 1.02 | 1.05 |
5HVX refinement based on a single data set taken from a single crystal, 5HVD refinement based on two data sets collected from a single crystal.
Rmerge=Σ(I−<I>)/Σ<I>
Rwork=Σ(|Fobs|−|Fcalc|)/Σ|Fobs| for 95% of the data. Rfree is the same definition but for the 5% of the data excluded from refinement.
*Values in parentheses are for highest-resolution shell.