Table 1.
Data collection, phasing, and refinement statistics for SAD structures
| Cu+-free Ctr1 (Ta6Br12 derivative) | Ctr1-Cu+ (Cu edge) | Cu+-free Ctr1 (Zn edge) | |
|---|---|---|---|
| Data collection | |||
| Space group | H32 | H32 | H32 |
| Cell dimensions | |||
| a, b, c (Å) | a = b = 73.848 | a = b = 73.451 | a = b = 73.764 |
| c = 410.577 | c = 409.105 | c = 408.873 | |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Wavelength | 1.2546 | 1.3776 | 1.2820 |
| Resolution (Å) | 3.0 | 3.2 | 3.5 |
| Rsym or Rmerge | 0.121 (1.578) | 0.083 (1.178) | 0.087 (0.931) |
| I / σI | 16.8 (1.3) | 21.7 (1.2) | 17.2 (1.8) |
| Completeness (%) | 99.3 (99.0) | 99.6 (99.7) | 99.7 (100) |
| Redundancy | 5.5 (5.4) | 6.9 (6.0) | 6.0 (6.2) |
| Refinement | |||
| Resolution (Å) | |||
| Low | 20 | 20 | |
| High (a*, b*, c*)a | 3.4, 3.5, 3.0 | 3.6, 3.6, 3.2 | |
| No. reflections | 6911 | 5931 | |
| Completeness (%)b | 77.8 | 79.9 | |
| Rwork / Rfree | 0.280 / 0.332 | 0.301 / 0.340 | |
| No. atoms | |||
| Protein | 1622 | 1560 | |
| Ligand/ion | 37 | 3 | |
| B-factors | |||
| Protein | 75.93 | 114.68 | |
| Ligand/ion | 95.87 | 116.89 | |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.008 | 0.009 | |
| Bond angles (°) | 1.315 | 1.152 | |
*A single crystal was used for each structure determination. *Values in parentheses are for highest-resolution shell. Rfree was calculated with 10% of the data
aReflections beyond these limits were excluded from refinement after anisotropic correction (a*, b*, and c* indicate reciprocal cell directions)
bCompleteness after anisotropic correction