TABLE 2.
X-ray crystallographic data collection and refinement statistics for E. coli PBP1b complexes
| Complex | PBP1b-cephalexin | PBP1b-CENTA | PBP1b-aztreonam | PBP1b-ampicillin |
|---|---|---|---|---|
| Data collection | ||||
| Wavelength (Å) | 1.00 Å | 1.00 Å | 1.00 Å | 1.00 Å |
| Space group | P22121 | P22121 | P22121 | P22121 |
| Cell dimensions | ||||
| a, b, c (Å) | 62.7, 63.8, 297.6 | 62.3, 63.9, 294.6 | 62.5, 64.4, 301.4 | 62.4, 63.8, 299.4 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å)a | 63.76–2.36 (2.42–2.36) | 62.49–2.31 (2.37–2.31) | 64.39–2.42 (2.48–2.42) | 74.8–2.70 (2.85–2.70) |
| Completeness (%)a | 98.7 (99.5) | 92.5 (85.9) | 96.7 (83.6) | 99.9 (100.0) |
| Unique reflectionsa | 49,407 (3638) | 48,263 (3270) | 45,993 (2868) | 33,979 (4857) |
| Redundancya | 4.7 (4.6) | 4.0 (2.6) | 3.5 (2.5) | 6.2 (6.4) |
| I/σ(I) a | 13.2 (2.2) | 13.5 (2.4) | 12.7 (1.9) | 10.4 (2.7) |
| Rmerge (%)a | 0.090 (0.650) | 0.067 (0.410) | 0.058 (0.552) | 0.098 (0.604) |
| Refinement statistics | ||||
| Ligand occupancy β-lactam, moenomycin | 1.00, 1.00 | 1.00, 1.00 | 1.00, 1.00 | 1.00, 1.00 |
| Rwork/Rfree | 0.235/0.250 | 0.253/0.279 | 0.235/0.274 | 0.256/0.285 |
| No. of atoms | ||||
| Protein | 5490 | 5063 | 5765 | 5461 |
| Ligand | 71 | 92 | 77 | 101 |
| Water | 223 | 187 | 233 | 107 |
| r.m.s.d. bonds (Å) | 0.014 | 0.012 | 0.013 | 0.010 |
| r.m.s.d. angles (°) | 1.75 | 1.77 | 1.82 | 1.20 |
| Average B-factors (Å2) | ||||
| Protein | 54.0 | 62.4 | 63.0 | 80.1 |
| Ligand | 98.5 | 103.6 | 106.2 | 85.7 |
| Water | 47.3 | 37.4 | 62.40 | 58.7 |
| Ramachandran statistics | ||||
| Favored (%) | 93.0 | 97.0 | 93.0 | 94.0 |
| Additional (%) | 6.6 | 2.8 | 6.4 | 5.8 |
| Disallowed (%) | 0.4 | 0.2 | 0.6 | 0.2 |
a The values in parentheses represent the highest resolution shell.