Table 2.
Crystallographic Data collection and refinement statistics.
| Data collection | EntE-B |
|---|---|
| Resolution | 40–3.1 Å |
| Space Group | P21 |
| Unit Cell | a=160.6 Å |
| b=101.8 Å | |
| c=240.7 Å | |
| β = 107.1° | |
| Rmergea | 6.8 % (47.5 %) |
| Completenessa | 99.4% (100.0%) |
| I/σa | 13.0 (1.8) |
| Redundancya | 3.7 (3.7) |
| Refinement | |
|---|---|
| Rcryst (Overall/Highest Resolution Shell)a | 21.8% (35.5%) |
| Rfree (Overall/Highest Resolution Shell)a | 26.4% (34.5%) |
| Wilson B-factor | 90.4 Å2 |
| Average B-Factor, Proteinb | 97.6 Å2 |
| Average B-Factor, Ligand, | 89.6 Å2 |
| Number of iodide ions | 25 |
| RMS Deviation bond lengths, angles | 0.01 Å, 1.36° |
a
Highest resolution Shell. Because of the high non-crystalographic symmetry, Rfree reflections were generated in thin shells. The high resolution Rfree value is reported for data from 3.33–3.29 Å.