6P56
Crystal structure of the transpeptidase domain of a T498A mutant of PBP2 from Neisseria gonorrhoeae
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 | 2019-02-06 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.922, 77.018, 87.172 |
| Unit cell angles | 90.00, 90.55, 90.00 |
Refinement procedure
| Resolution | 34.010 - 1.920 |
| R-factor | 0.187 |
| Rwork | 0.185 |
| R-free | 0.23400 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.281 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | FFT |
| Refinement software | REFMAC (5.8.0218) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.010 | 1.950 |
| High resolution limit [Å] | 1.920 | 1.920 |
| Rmerge | 0.135 | 0.741 |
| Rpim | 0.062 | 0.383 |
| Number of reflections | 41093 | 2035 |
| <I/σ(I)> | 23.2 | 2.1 |
| Completeness [%] | 96.0 | 97.4 |
| Redundancy | 5.3 | 4.2 |
| CC(1/2) | 0.993 | 0.708 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.3 | 291 | 0.1 M CHES, 40% PEG600 |
