9OTG
Crystal structure of the transpeptidase domain of PBP2 from Neisseria gonorrhoeae strain FA19 acylated by piperacillin
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 | 2022-02-25 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.986, 77.962, 87.237 |
| Unit cell angles | 90.00, 90.75, 90.00 |
Refinement procedure
| Resolution | 39.000 - 3.150 |
| R-factor | 0.159 |
| Rwork | 0.153 |
| R-free | 0.26600 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.382 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.000 | 3.260 |
| High resolution limit [Å] | 3.150 | 3.150 |
| Rmerge | 0.128 | 0.668 |
| Rpim | 0.075 | 0.391 |
| Number of reflections | 10473 | 1053 |
| <I/σ(I)> | 11.9 | 3.3 |
| Completeness [%] | 99.0 | |
| Redundancy | 3.9 | 4 |
| CC(1/2) | 0.992 | 0.731 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 35-40% PEG 600 and 0.1 M CHES |
