Table 2.
Data-collection and refinement statistics. Values in parentheses are for the outer shell.
| Data Collection | LpxA |
|---|---|
| Ligand added | Peptide CR20 |
| Data collection | |
| Wavelength (Å) | 1.5415 |
| Resolution range (Å) | 21.65–1.60 (1.69–1.60) |
| Space group | P213 |
| a = b = c (Å) | 96.73 |
| CC1/2 (%) | 94.80 (76.70) |
| Unique reflections | 34668 (2647) |
| Completeness (%) | 99.84 (100) |
| Mean I/σ(I) | 14.2(3.9) |
| Wilson B factor (Å2) | 23.684 |
| R merge a | 0.078 (0.085) |
| Refinement | |
| R factor b | 0.1910 (0.453) |
| R free c | 0.2260 (0.3850) |
| No. of atoms | 2500 |
| No. of waters | 400 |
| No. of protein residues | 274 |
| R.m.s.d., bonds (Å) | 0.007 |
| R.m.s.d., angles (°) | 1.091 |
| Ramachandran favored (%) | 98.5 |
| Ramachandran outliers (%) | 0 |
| B factors (Å 2 ) | |
| Protein | 23.68 |
| Ligand | 25.68 |
| Solvent | 38.90 |
| All-atom clash score | 2.85 |
| Molprobity score | 1.07 (99th percentile) |
Resolution limit was defined as the highest resolution shell where the average I/σ(I) was 2.
aRmerge = ΣhklΣi|Ii(hkl) − <I(hkl)>|/ΣhklΣiI(hkl).
bRfactor = Σ|Fo − Fc|/ΣFo. Five percent of the reflections was used to calculate cRfree.