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 |