Table 1.
Data collection and refinement statistics
| Statisticsa | Nsp7/SeMet-Nsp8b |
|
|---|---|---|
| Crystal 1 | Crystal 2c | |
| Data collection | ||
| X-ray source | BL14.2, BESSY (Berlin, Germany) | |
| Wavelength (Å) | 0.9809 | 0.97974/0.97990 |
| Space group | C2221 | |
| Unit cell dimensions (Å) | a = 121.45; b = 160.30; c = 102.66 | a = 120.78; b = 161.43; c = 103.25 |
| Resolution range (Å) | 33.45–2.60 (2.70–2.60) | 33.55–3.24 (3.34–3.24) |
| No. of unique reflections | 31,155 | 16,370/16,291 |
| Completeness (%) | 99.8 (100) | 99.8 (99.9)/99.7 (99.3) |
| Mean I/σ(I) | 20.38 (3.33) | 24.74 (4.92)/23.52 (3.62) |
| Multiplicity | 7.23 (7.41) | 14.48 (14.99)/14.60 (14.90) |
| Rint (%) | 5.77 (62.0) | 7.81 (48.4)/8.42 (84.1) |
| Rsigma (%) | 3.1 (30.0) | 2.84 (19.9)/2.81 (27.08) |
| Solvent content (%) | 61.42 | |
| Vm (Å3/Da) | 3.19 | |
| Refinement | ||
| Resolution range | 33.45-2.60 | |
| Rwork (%) | 20.51 | |
| Rfree (%) | 22.74 | |
| Modeled residues | A: −2–73, 79–192; B: 2–83; C: 0–81; D: −2–191; E: 2–82; F: 0–77 | |
| No. of protein atoms | 5,498 | |
| No. of water molecules | 77 | |
| RMSD in bond lengths (Å) | 0.010 | |
| RMSD in bond angles (°) | 1.29 | |
| Ramachandran plot (%) | ||
| Mostly favored | 97.3 | |
| Additionally allowed | 2.4 | |
| Outliers | 0.3 | |
a
Rint = Σ||Fo|2 − <|Fo|2>| |/Σ|Fo|2. |Fo|2 values are the intensities of the reflections in the unmerged data. <|Fo|2> is the mean intensity for symmetry equivalents, including Friedel pairs. Rsigma = Σ[σ (|Fo|2)]/Σ[|Fo|2]. The |Fo|2 values are the intensities of the reflections in the unique data. R = Σ||Fo| − |Fc||/Σ|Fo|. The |Fo| values are the amplitudes of the structure factors. Rwork is the R value for reflections used in refinement, whereas Rfree is the R value for 5% of the reflections which are selected in thin shells and are not included in the refinement.
b
Values in parentheses represent the highest-resolution shell.
c
Values are presented as “peak/inflection” where applicable.