6P52
Crystal structure of transpeptidase domain of PBP2 from Neisseria gonorrhoeae with a bound phosphate at the active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-08-12 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.973, 76.868, 86.470 |
| Unit cell angles | 90.00, 92.32, 90.00 |
Refinement procedure
| Resolution | 38.350 - 1.830 |
| R-factor | 0.197 |
| Rwork | 0.195 |
| R-free | 0.23300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4u3t |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.269 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0218) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.350 | 1.860 |
| High resolution limit [Å] | 1.830 | 1.830 |
| Rmerge | 0.071 | 0.932 |
| Rpim | 0.029 | 0.394 |
| Number of reflections | 48725 | 2394 |
| <I/σ(I)> | 42.5 | 2 |
| Completeness [%] | 99.6 | 99.2 |
| Redundancy | 6.8 | 6.5 |
| CC(1/2) | 0.678 | 0.764 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.3 | 291 | 40% PEG600, 0.1 M CHES |
