7K3M
Crystal Structure of the Beta Lactamase Class D from Chitinophaga pinensis by Serial Crystallography
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 295 |
| Detector technology | PIXEL |
| Collection date | 2019-11-12 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.413, 69.347, 70.035 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.280 - 1.800 |
| R-factor | 0.1829 |
| Rwork | 0.177 |
| R-free | 0.22430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | The crystal structure of the same protein in the complex with avibactam which will be deposited |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.580 |
| Data reduction software | DIALS |
| Data scaling software | PRIME |
| Phasing software | MOLREP (11.7.02) |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.280 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.670 | 0.850 |
| Number of reflections | 23276 | 1134 |
| <I/σ(I)> | 2.81 | 0.76 |
| Completeness [%] | 100.0 | 99.8 |
| Redundancy | 79.11 | |
| CC(1/2) | 0.970 | 0.730 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 295 | 0.1 M Bis-Tris propane pH 9.0, 8 %(w/v) PEG20000 |
