TABLE 1.
Crystallographic X-ray diffraction and refinement statistics
| Statistic | Value for M2e peptide + Fab148 |
|---|---|
| Data statistics | |
| Wavelength (Å) | 1.000 |
| No. of reflections (unique reflections) | 326,286 (95,371) |
| Resolution range (Å) | 50.0∼2.20 (2.26∼2.20) |
| Completeness (%) | 97.1 (84.1) |
| Rmerge (%)a | 6.9 (33.6) |
| I/σ | 11.8 (3.5) |
| Space group | C2221 |
| Unit cell parameters (Å) | a = 92.6, b = 101.4, c = 212.5 |
| α = β = γ = 90° | |
| Refinement statistics | |
| Resolution range (Å) | 49.2∼2.2 |
| No. of reflections | 47,639 |
| R/Rfree (%)b | 18.7/24.0 |
| RMS deviationc | |
| Bonds (Å) | 0.024 |
| Angles (°) | 2.26 |
| No. of water molecules | 309 |
| Average B (Å2) | 29.4 |
| Ramachandran statistics (%)d | |
| Favored | 97.6 |
| Allowed | 2.4 |
| Outlier | 0.0 |
a
Rmerge = Σ|I − <I>|/Σ<I>, where I and <I> are the measured and averaged intensities of multiple measurements of the same reflection, respectively. The summation is over all the observed reflections.
b
R = Σ|Fo − Fc|/Σ|Fo|, calculated for all observed data. Rfree = Σ|Fo − Fc|/Σ|Fo|, calculated for a specified number of randomly chosen reflections that were excluded from the refinement.
c
RMS, root mean square.
d
Calculated using RAMPAGE (23).