Table 1.
Data collection, phasing and structural refinement statistics of the CusC, ΔC1 and C1S proteins.
| CusC (WT) | ΔC1 | ΔC1 (SeMet) | C1S | |
|---|---|---|---|---|
| Data Collection | ||||
| Space group | R32 | P21 | P21 | P21 |
| Cell dimensions | ||||
| a, b, c (Å) | 88.49, 88.49, 474.72.60 | 62.02, 104.47, 72.03 | 61.93, 104.41, 71.95 | 61.88, 105.03, 72.36 |
| α, β, γ (°) | 90, 90, 120 | 90, 101.03, 90 | 90, 101.03, 90 | 90, 101.06, 90 |
| Wavelength (Å) | 0.979 | 0.979 | 0.979 | 0.979 |
| Resolution (Å) | 50-2.09 (2.17–2.09) | 50-2.53 (2.63–2.53) | 50-2.8 (2.90–2.80) | 50-2.69 (2.84–2.69) |
| Rsym (%) | 8.3 (40.4) | 6.9 (41.7) | 11.6 (45.9) | 10.2 (30.4) |
| Average I/σI | 12.7 (1.8) | 12.1 (1.7) | 10.5 (2.16) | 9.3 (3.4) |
| Completeness (%) | 97.3 (97.2) | 94.0 (91.6) | 99.9 (99.8) | 98.5 (95.0) |
| Redundancy | 2.4 (2.4) | 2.1 (2.0) | 2.8 (2.8) | 3.8 (3.7) |
| Total reflections | 640,300 | 426,465 | 654,832 | 94,904 |
| Unique reflections | 43,397 | 30,236 | 22,466 | 24,874 |
| Phasing | ||||
| Number of sites | 10 | |||
| Figure of merit (acentric/centric) | 0.821/0.797 | |||
| Refinement | ||||
| Resolution (Å) | 50-2.09 | 50-2.53 | 50-2.69 | |
| No. reflections | 54,129 | 31,197 | 24,838 | |
| Rwork/Rfree (%) | 20.60/23.50 | 20.77/26.71 | 19.08/24.61 | |
| B-factors (Å2) | ||||
| Protein chain A | 30.6 | 43.7 | 46.3 | |
| Protein chain B | 50.7 | 51.8 | ||
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.007 | 0.008 | 0.009 | |
| Bond angles (°) | 0.924 | 1.105 | 1.143 | |
| Ramachandran | ||||
| most favored | 96.4 | 93.4 | 92.8 | |
| additional allowed | 3.6 | 6.6 | 6.2 | |
| generously allowed | 0 | 0 | 0.7 | |
| disallowed | 0 | 0 | 0.3 | |