Table 2. Crystallographic Data Collection and Refinement Statisticsa.
| Data Collection | |
| resolution (highest-resolution shell) (Å) | 24.78–2.60 (2.68–2.60)b |
| X-ray source | X25, NSLS |
| wavelength (Å) | 0.979 |
| space group | R32 |
| cell dimensions (Å) | a = b = 156.97, c = 121.95 |
| no. of reflections observed (unique) | 896022 (17137) |
| completeness (%) | 98.9 (99.1) |
| Rmerge (%)b | 18.8 (47.1) |
| I/σ(I) | 13.6 (2.4) |
| redundancy | 9.8 (8.2) |
| Refinement | |
| no. of protein residues/water atoms per asymmetric unit | 375/233 |
| no. of other ligands per asymmetric unit | 2 Co(II), 1 oxalate |
| no. of reflections (work/free) | 17122/1712 |
| Rwork, Rfree (%) | 17.5, 22.4 |
| resolution (Å) | 24.78–2.60 |
| average B factor (Å2) | 37.9 |
| protein (Å2) | 35.2 |
| Co(II) (Å2) | 37.2 |
| oxalate (Å2) | 40.9 |
| water (Å2) | 39.1 |
| rmsd for bond lengths (Å) | 0.008 |
| rmsd for bond angles (deg) | 1.105 |
a
Data for the highest-resolution shell are given in parentheses.
b
Rmerge = ∑hkl∑i|Ihkl,i – ⟨Ihkl⟩I|/∑hkl∑i|Ihkl,i|, where ⟨Ihkl⟩ is the mean intensity of the multiple Ihkl,i observations for symmetry-related reflections.