38HJ
Crystal structure of the transpeptidase domain of a Y422F mutant of PBP2 from Neisseria gonorrhoeae strain H041 acylated by cefoperazone
This is a non-PDB format compatible entry.
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 | 2025-10-31 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.600, 61.600, 110.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.100 - 2.600 |
| Rwork | 0.227 |
| R-free | 0.29200 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.700 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | FFT |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.100 | 2.640 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.181 | 0.470 |
| Rpim | 0.072 | 0.185 |
| Number of reflections | 10328 | 548 |
| <I/σ(I)> | 16.5 | 1.7 |
| Completeness [%] | 92.6 | 99.6 |
| Redundancy | 6.8 | |
| CC(1/2) | 0.968 | 0.909 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.1 | 291 | 0.1 M CHES buffer, pH 9.1 to 10.1, and 32-42% PEG 600 |
