Table 2. Crystallographic data and refinement statistics for CatchER complexes.
| CatchER(apo) | CatchER-Ca2+ | CatchER-Gd3+ | |
|---|---|---|---|
| X-ray source | APS 22ID | APS 22ID | APS 22BM |
| Wavelength (Å) | 0.8 | 0.8 | 1.0 |
| Temperature (K) | 100 | 100 | 100 |
| Space group | C2221 | P212121 | C2221 |
| Unit-cell parameters (Å) | a = 61.40, b = 88.53, c = 118.43 | a = 54.24, b = 61.06, c = 67.40 | a = 61.06, b = 88.33, c = 118.17 |
| Protein molecules per asymmetric unit | 1 | 1 | 1 |
| Unique reflections | 38048 | 70349 | 30260 |
| R merge † (%) | 6.8 (22.8) | 8.1 (39.2) | 8.5 (18.5) |
| 〈I/σ(I)〉† | 22.6 (7.7) | 19.9 (6.1) | 14.2 (8.7) |
| Resolution range (Å) | 31.08–1.66 | 50–1.20 | 27.13–1.78 |
| Completeness† (%) | 99.1 (93.6) | 99.2 (100) | 98.3 (93.8) |
| R work | 0.181 | 0.150 | 0.196 |
| R free | 0.203 | 0.191 | 0.219 |
| No. of protein atoms (includes alternative conformations) | 1956 | 1967 | 1922 |
| No. of H2O molecules (total occupancies‡) | 167 (151) | 197 (191.5) | 138 (128.5) |
| No. of ions (occupancy) | 1 (1.0) | 2 (0.5/0.5) | 2 (0.7/0.3) |
| R.m.s. deviation from ideality | |||
| Bonds (Å) | 0.012 | 0.012 | 0.014 |
| Angle distance | 1.527 ŧ | 0.031°¶ | 1.594 ŧ |
| Average B factors (Å2) | |||
| Main-chain atoms | 17.46 | 16.60 | 20.40 |
| Side-chain atoms | 19.34 | 20.52 | 22.01 |
| H2O | 25.47 | 28.80 | 25.79 |
| Ions | 43.74 | 35.67 | 37.56 |
| Ramachandran plots results, residues in | |||
| Favored region | 221 (98.2%) | 220 (98.7%) | 221 (98.2%) |
| Allowed region | 4 (1.8%) | 3 (1.3%) | 4 (1.8%) |
†
Values in parentheses are for the highest resolution shell.
‡
Total occupancies are the sum of calculated occupancies of all the atoms or ions.
§
The angle r.m.s.d. in REFMAC5.2 is indicated by angle in degrees.
¶
The angle r.m.s.d. in SHELX-97 is indicated by distance in Å.