Table 1.
Crystallographic data collection and refinement statistics.a
| Data Collection | |
|---|---|
| Resolution (highest resolution shell) (Å) | ∞-2.31 (2.40–2.31) |
| X-ray Source | CuKα |
| Wavelength (Å) | 1.5418 |
| Space Group | R32 |
| Cell dimension (Å) | a = b = 154.76, c = 121.50 |
| Reflections observed (unique) | 141418 (46701) |
| Completeness (%) | 99.8 (100) |
| Rmerge (%)b | 18.6 (34.3) |
| I/σ (I) | 5.4 (2.3) |
| Redundancy | 5.7 (4.1) |
| Refinement | |
| Protein residues/water atoms per asu | 377/392 |
| Other ligands per asu | 8 |
| Reflections (work/free) | 41624/2114 |
| Rwork/Rfree (%) | 18.9/25.3 |
| Resolution (Å) | 23.61–2.31 |
| Average B-factor (Å2) | 7.1 |
| Protein (Å2) | 7.0 |
| Mn(II) (Å2) | 10.9 |
| Carbonate(Å2) | 3.1 |
| Water (Å2) | 15.8 |
| RMSDc Bond lengths (Å) | 0.006 |
| RMSD Bond angles (°) | 1.009 |
a
Data for the highest resolution shell is in parenthesis.
b
Rmerge = Σhkl Σi| Ihkl, i-<Ihkl> I | / ΣhklΣi | Ihkl, i |, where <Ihkl> is the mean intensity of the multiple Ihkl, i observations for symmetry-related reflections.
c
RMSD: root mean square deviation.