Table 1. Crystallographic statistics.
| Statistics | Edge | Peak | Remote |
|---|---|---|---|
| Data collection | |||
| Crystal/space group | TcdA-f1/P41212 | ||
| Unit cell lengths, Å | 42.05 × 42.05 × 132.11 | ||
| Unit cell angles,° | 90, 90, 90 | ||
| Wavelength, Å | 0.979741 | 0.979571 | 1.019867 |
| Resolution, Å | 40.16-1.85 | 40.16-1.85 | 40.16-1.85 |
| High resolution, Å | 1.92-1.85 | 1.92-1.85 | 1.92-1.85 |
| Total reflections* | 69,718 (6,383) | 69,632 (6,321) | 70,319 (6,608) |
| Unique reflections* | 10,802 (1,020) | 10,798 (1,015) | 10,812 (1,031) |
| Completeness, %* | 99.2 (96.1) | 99.2 (95.7) | 99.3 (97.2) |
| I/σ* | 26.5 (8.7) | 21.4 (7.4) | 31.6 (11.0) |
| Rsym*† | 0.046 (0.182) | 0.057 (0.187) | 0.038 (0.158) |
| Refinement | |||
| Resolution, Å | 40.16-1.85 (1.90-1.85) | ||
| Rwork‡ | 0.160 (0.135) | ||
| Rfree§ | 0.205 (0.175) | ||
| Number of atoms | |||
| Protein | 988 | ||
| Solvent and Ions | 218 | ||
| rms deviations from ideal geometry | |||
| Bond lengths, Å | 0.007 | ||
| Bond angles, ° | 1.00 | ||
| Average B factor, Å2 | 13.8 | ||
*
Values from the outermost resolution shell are given in parentheses.
†
Rsym = ΣhΣi(|Ii(h) — 〈I(h) 〉|)/ΣhΣiIi(h), where Ii(h) is the ith integrated intensity of a given reflection, and 〈I(h) 〉 is the weighted mean of all measurements of I(h).
‡
Rwork = Σh∥F(h)o|—|F(h)c∥/Σh|F(h)o| for the 95% of reflection data used in refinement.
§
Rfree = Σh∥F(h)o|—|F(h)c∥/Σh|F(h)o| for the 5% of reflection data excluded from ref inement.