Table 2.
X-ray data and refinement statistics
| Cya2 | |
|---|---|
| Space group | P21 |
| Unit cell constants | a = 62.4 Å, b = 84.1 Å, c = 115.3 Å; β = 97.4 |
| Resolution, Å | 50.0–2.3 |
| Unique reflections | 50,776 |
| 〈I/σ〉 | 8.4 |
| Completeness, % | 97.3 (85.0) |
| Rmerge,* % | 8.0 (37.9) |
| Refinement resolution, Å | 20.0–2.3 |
| Total reflections used | 48,079 |
| Final Rcryst/Rfree,†‡ % | 19.4/28.2 |
| Atoms: protein/solvent | 8,911/468 |
| rmsd bond lengths, Å | 0.02 |
| rmsd bond angles, ° | 1.9 |
| rmsd bonded B, Å2 | 1.6 |
| Average B-factor: protein /solvent, Å2 | 41/48 |
Numbers in parentheses are for the outermost shell.
*Rmerge = Σ I − 〈I〉/Σ I; I is the intensity of an individual measurement, and 〈I〉 is the corresponding mean value.
†R-factor = Σ||Fobs| − k|Fcalc||/Σ|Fobs|; |Fobs| is the observed and |Fcalc| the calculated structure factor amplitude.
‡Rfree was calculated from 5% of measured reflections omitted from refinement.