4OQI
Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying R164S/G238S mutations
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 152.930, 46.400, 34.430 |
Unit cell angles | 90.00, 93.22, 90.00 |
Refinement procedure
Resolution | 44.400 - 1.130 |
R-factor | 0.124 |
Rwork | 0.122 |
R-free | 0.15500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.022 |
RMSD bond angle | 2.181 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.240 | 1.200 |
High resolution limit [Å] | 1.130 | 1.130 |
Number of reflections | 82624 | |
<I/σ(I)> | 11.98 | 4.46 |
Completeness [%] | 85.7 | |
Redundancy | 3.57 | 3.18 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.2 | 293 | 9% (wt/vol) polyethylene glycol (PEG) 8000, 100 mM MES, and 200mM Ca(OAc)2, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |