6P53
Crystal structure of the transpeptidase domain of PBP2 from Neisseria gonorrhoeae in apo form
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 | 2018-02-20 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.334, 77.254, 88.007 |
| Unit cell angles | 90.00, 91.85, 90.00 |
Refinement procedure
| Resolution | 36.090 - 1.920 |
| R-factor | 0.184 |
| Rwork | 0.181 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4u3t |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.437 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0218) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.090 | 1.950 |
| High resolution limit [Å] | 1.920 | 1.920 |
| Rmerge | 0.052 | 0.413 |
| Rpim | 0.022 | 0.191 |
| Number of reflections | 42141 | 2272 |
| <I/σ(I)> | 33.9 | 3.3 |
| Completeness [%] | 90.8 | 97.3 |
| Redundancy | 6.3 | 5.4 |
| CC(1/2) | 1.000 | 0.930 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.3 | 291 | 40% PEG600, 0.1 M CHES |
