Table 1. Crystallographic data collection and refinement statistics.
| SceCD | SceCD Thimerosal | SceCD Eu | HsaBT-CD | HsaBT-CD Cd2+ | CthCD-CTCter1 | CthCD-CTCter2 | CthCD-CT | CthΔBCCP | |
|---|---|---|---|---|---|---|---|---|---|
| Data collection | |||||||||
| Space group | P43212 | P43212 | P43212 | I4122 | I4122 | P212121 | P212121 | P31212 | P6422 |
| Cell dimensions | |||||||||
| a, b, c (Å) | 110.86, 110.86, 131.12 | 111.22, 111.22, 131.49 | 108.65, 108.65, 127.36 | 267.27, 267.27, 210.61 | 267.67, 267.67, 210.46 | 97.66, 165.34, 219.23 | 100.17, 153.45, 249,24 | 295.02, 295.02, 189.52 | 462.20, 462.20, 204.64 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 120 | 90, 90, 120 |
| Resolution* (Å) | 3.0 | 3.4 | 4.0 | 3.7 | 4.1 | 3.6 | 4.5 | 7.2 | 8.4 |
| RMerge† | 18.2 (389.6) | 20.5 (306.1) | 40.6 (327.0) | 7.5 (400.9) | 15 (730.5) | 14.5 (384.5) | 27.4 (225.6) | 5.6 (302.6) | 29.4 (381.7) |
| CC ½*,† | 100 (58.3) | 99.9 (42.6) | 99.9 (48.5) | 100 (59.4) | 99.8 (73.2) | 99.9 (50.9) | 99.5 (46.7) | 100 (33.3) | 99.7 (35) |
| I/σI† | 24.68 (1.46) | 7.99 (0.89) | 17.92 (1.85) | 21.24 (1.07) | 16.53 (1.41) | 10.61 (0.97) | 6.35 (1.00) | 18.95 (0.92) | 9.05 (0.9) |
| Completeness† | 99.9 (99.9) | 99.6 (100) | 99.7 (96.8) | 99.8 (99.1) | 99.8 (99.7) | 99.7 (99.9) | 99.4 (98.6) | 99.6 (100) | 99.1 (99.9) |
| Redundancy† | 39.1 (39.8) | 12.1 (14.3) | 81.6 (65.2) | 13.7 (13.7) | 20.9 (19.1) | 12.7 (13.5) | 6.1 (6.5) | 9.9 (10.4) | 18.5 (18.2) |
| Refinement | |||||||||
| Resolution* (Å) | 46.4–3.0 | 84.5–3.7 | 49.2–3.6 | 49.1–4.5 | 49.9–7.2 | 50.0–8.4 | |||
| Reflections | 16,928 | — | — | 40,647 | — | 41,799 | 23,340 | 14,046 | 12,111 |
| Rwork/Rfree | 0.20/0.24 | — | — | 0.35/0.38‡ | — | 0.20/0.24 | 0.24/0.24 | 0.23/0.25 | 0.30/0.32 |
| Number of atoms | |||||||||
| Protein | 5,465 | 6,925 | 16,592 | 16,405 | 22,543 | 22,445 | |||
| Waters | 43 | — | — | — | — | — | — | — | — |
| Ligand/ion | 7 | — | — | 5 | — | — | — | — | — |
| B-factors | |||||||||
| Protein | 130 | 158 | 226 | 275 | 272 | 250 | |||
| Waters | 84 | — | — | — | — | — | — | — | — |
| Ligand/ion | 90 | — | — | 189 | — | — | — | — | — |
| R.m.s.d. | |||||||||
| RMS (angles, °) | 0.97 | — | — | 0.83 | — | 1.07 | 1.11 | 1.15 | 1.01 |
| RMS (bonds, Å) | 0.01 | — | — | 0.01 | — | 0.01 | 0.01 | 0.01 | 0.01 |
*Resolution cutoffs determined based on internal correlation significant at the 0.1% level as calculated by XDS.
†Highest-resolution shell is shown in parentheses.
‡Modelled only as poly-alanine.