Table 1. Crystallographic data collection and refinement statistics.
|
Data collection | |
| Beamline | SSRF BL17U |
| Wavelength | 0.9796 Å |
| Space group | C 2 2 21 |
| Cell dimensions | |
| a, b, c (Å) | 131.79.174.14.198.82 |
| α, β, γ (°) | 90, 90, 90 |
| Resolution (Å) | 50.00–3.00 (3.07–3.00) |
| Rmerge (%) | 9.4 (86.3) |
| I/σI | 15.5 (1.6) |
| Completeness (%) | 99.7 (99.8) |
| Redundancy | 5.3 |
| Refinement | |
| Resolution (Å) | 46.85–3.00 (3.07–3.00) |
| No. Reflections | 43883 |
| Rwork/Rfree (%) | 22.7/29.5 |
| No. atoms | |
| Protein | 12029 |
| Cd cation | 29 |
| B-factor (Å2) | |
| Protein | 113.7 |
| Cd cation | 207.8 |
| r.m.s. deviations | |
| Bond lengths (Å) | 0.014 |
| Bond angles (°) | 1.53 |
| Ramachandran plot (%) | |
| Most favored | 96.6 |
| Additionally allowed | 2.2 |
| Generously allowed | 0.6 |
| Disallowed | 0.6 |
Rwork and Rfree are defined as:
R = Σ hkl||Fobs| − |Fcalc||/Σ hkl|Fobs|, where h, k, and l are the indices of the reflections.