Table 1.
X-ray crystallographic data collection and refinement statistics of E. coli PBP1b in complex with EFtsN
| PBP1b–EFtsN | |
|---|---|
| Data collection | |
| Space group | P21212 |
| a, b, c (Å) | 63.1, 283.0, 62.7 |
| α, β, γ (°) | 90, 90, 90 |
| Resolution range (Å)a | 47.2–2.4 (2.51–2.4) |
| /<σI>a | 8.1 (1.5) |
| Completeness elliptical (%)a | 95.5 (85.9) |
| Completeness spherical (%)a | 57.1 (22.3) |
| Redundancya | 8.5 (7.2) |
| Refinement | |
| Resolution range (Å) | 47.2–2.4 |
| No. of unique reflections | 25,830 |
| Rwork (%) | 22.5 |
| Rfree (%) | 25.6 |
| No. atoms | |
| Protein | 5525 |
| Ligands | 77 |
| Water | 55 |
| RMSDs from ideal stereochemistry | |
| Bond lengths (Å) | 0.01 |
| Bond angles (°) | 1.5 |
| Mean B factor (Å2) | |
| Protein | 78.2 |
| Ligands | 150 |
| Water | 36.1 |
| Ramachandran plot (%) | |
| Favored region | 94.2 |
| Allowed regions | 5.4 |
| Outlier regions | 0.4 |
a
Values in parentheses are related to high resolution shell.