6P54
Crystal structure of transpeptidase domain of PBP2 from Neisseria gonorrhoeae acylated by ceftriaxone
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 | 2019-02-07 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.223, 78.485, 87.608 |
| Unit cell angles | 90.00, 91.34, 90.00 |
Refinement procedure
| Resolution | 35.010 - 1.830 |
| R-factor | 0.174 |
| Rwork | 0.172 |
| R-free | 0.21000 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.652 |
| 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] | 35.010 | 1.860 |
| High resolution limit [Å] | 1.830 | 1.830 |
| Rmerge | 0.087 | 0.643 |
| Rpim | 0.041 | 0.335 |
| Number of reflections | 50936 | 2469 |
| <I/σ(I)> | 29.1 | 2 |
| Completeness [%] | 98.8 | 97.2 |
| Redundancy | 5.2 | 3.9 |
| CC(1/2) | 0.997 | 0.801 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.3 | 291 | 0.1 M CHES, 40% PEG600 |
