8VBZ
Crystal structure of the transpeptidase domain of a S310A mutant of PBP2 from Neisseria gonorrhoeae strain H041
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-02-21 |
| Detector | DECTRIS EIGER2 S 16M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.487, 61.079, 109.419 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.880 - 1.900 |
| R-factor | 0.177 |
| Rwork | 0.175 |
| R-free | 0.21100 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.700 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.900 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.107 | 0.491 |
| Rmeas | 0.116 | 0.533 |
| Rpim | 0.045 | 0.204 |
| Number of reflections | 27372 | 1376 |
| <I/σ(I)> | 20.1 | 2.75 |
| Completeness [%] | 96.6 | 99.4 |
| Redundancy | 5.9 | 6.3 |
| CC(1/2) | 0.991 | 0.908 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 32-40% PEG 600, 0.1 M CHES |
