Table 1. Data collection and refinement statistics for B. subtilis S72N TRAP.
| Data collection | |
| Space group | P21212 |
| Unit cell | a = 109.4 Å, b = 110.2 Å, c = 46.2 Å |
| Resolution | 25–2.7 Å (2.80–2.70 Å) |
| No. of reflections | 14253 (1025) |
| Redundancy | 6.3 (4.2) |
| R merge a, % | 9.7 (50.2) |
| Completeness, % | 91.9 (68.2) |
| I/σ | 15.3 (2.8) |
| Wilson B factor | 86.1 |
| Refinement | |
| Resolution range | 25–2.72 Å (2.79–2.72 Å) |
| No. of reflections used in refinement | 13396 |
| No. of reflections excluded from refinement | 825 |
| R factorb, % | 20.9 (34.1) |
| Free R factorb, % | 24.5 (38.2) |
| Number of atoms | |
| Protein | 2952 |
| Ligand | 90 |
| Water molecules | 27 |
| Average B factor (protein) | 83.8 |
| Average B factor (solvent) | 82.5 |
| Rmsd bond lengths | 0.009 Å |
| Rmsd bond angles | 1.2° |
| Ramachandran plot | |
| Most favored regions, % | 97.8 |
| Additionally allowed regions, % | 2.2 |
Values in parentheses are for the highest resolution shell.
a
Rmerge = ∑hkl∑i|Ii(h) - <I(h)>|/∑hkl∑i Ii(h), where I(h) is intensity of reflection h, <I(h)> is average value of intensity, the sum ∑hkl is over all measured reflections and the sum ∑i is over i measurements of a reflection.
b
Crystallographic R = ∑hkl||Fobs - Fcalc||/∑hkl|Fobs|, Rfree was calculated using a randomly chosen set of reflections that were excluded from the refinement.