5LP5
Complex between Penicillin-Binding Protein (PBP2) and MreC from Helicobacter pylori
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 273 |
| Detector technology | CCD |
| Collection date | 2009-04-09 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.87260 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 338.656, 48.340, 151.513 |
| Unit cell angles | 90.00, 113.02, 90.00 |
Refinement procedure
| Resolution | 43.940 - 2.740 |
| R-factor | 0.25771 |
| Rwork | 0.257 |
| R-free | 0.29216 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5lp4 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.280 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.940 | 2.900 |
| High resolution limit [Å] | 2.740 | 2.740 |
| Rmerge | 0.410 | |
| Number of reflections | 52464 | |
| <I/σ(I)> | 19.84 | 3 |
| Completeness [%] | 86.5 | 83.1 |
| Redundancy | 2.8 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 5%W/V PEG6000, 50MM CITRIC ACID PH 5, 9MM ZNCL2 |
