1NZO
The crystal structure of wild type penicillin-binding protein 5 from E. coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-01-10 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 109.350, 50.280, 84.530 |
| Unit cell angles | 90.00, 120.90, 90.00 |
Refinement procedure
| Resolution | 14.920 - 1.850 |
| R-factor | 0.20964 |
| Rwork | 0.208 |
| R-free | 0.24503 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hd8 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.509 |
| Data reduction software | CrystalClear ((MSC/RIGAKU)) |
| Data scaling software | CrystalClear ((MSC/RIGAKU)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.060 | 0.323 |
| Number of reflections | 31624 | |
| <I/σ(I)> | 7.4 | 2 |
| Completeness [%] | 93.4 | 67.8 |
| Redundancy | 4.5 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 294 | 100mM Tris pH 7.0, 8% PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
