TABLE 2.
Crystallographic data collection and refinement of Tmm7211.
| Parameters | Tmm7211 | Tmm7211-5-min | Tmm7211-20-min |
| Diffraction data | |||
| Space group | P21 | P21 | P21 |
| Unit cell | |||
| a, b, c (Å) | 69.4, 82.1, 97.9 | 69.0, 81.8, 97.9 | 68.7, 81.7, 97.6 |
| α, β, γ (°) | 90.0, 98.1, 90.0 | 90.0, 98.1, 90.0 | 90.0, 98.5, 90.0 |
| Resolution range (Å) | 50.0–1.8 (1.83–1.80)* | 50.0–1.8 (1.86–1.80) | 50.0–2.0 (2.07–2.00) |
| Redundancy | 3.3 (3.3) | 6.4 (6.9) | 6.6 (6.3) |
| Completeness (%) | 98.1 (98.6) | 97.7 (98.6) | 100.0 (100.0) |
| R merge ** | 0.1 (0.4) | 0.1 (0.4) | 0.1 (0.6) |
| I/σI | 18.0 (1.8) | 49.8 (11.9) | 26.6 (3.7) |
| Refinement statistics | |||
| R-factor | 0.22 | 0.16 | 0.16 |
| Free R-factor | 0.25 | 0.18 | 0.20 |
| RMSD from ideal geometry | |||
| Bond lengths (Å) | 0.006 | 0.006 | 0.006 |
| Bond angles (°) | 1.1 | 1.2 | 1.1 |
| Ramachandran plot (%) | |||
| Favored | 93.8 | 94.7 | 94.7 |
| Allowed | 6.0 | 5.1 | 5.1 |
| Outliers | 0.2 | 0.2 | 0.2 |
| B-factors (Å2) | |||
| Protein | 29.7 | 23.7 | 31.5 |
| NADP+ | 25.1 | 21.8 | 28.7 |
| FAD | 23.2 | 18.5 | 27.3 |
| Water | 38.5 | 33.5 | 37.4 |
| All atoms | 30.6 | 24.9 | 32.0 |
*Numbers in parentheses refer to data in the highest-resolution shell.
** Rmerge = ΣhklΣi| I(hkl)i—< I(hkl) > | /ΣhklΣiI(hkl)i, where I is the observed intensity, < I(hkl) > represents the average intensity, and I(hkl)i represents the observed intensity of each unique reflection.