5HAR
OXA-163 beta-lactamase - S70G mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-14 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9970 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 44.340, 87.980, 124.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 62.380 - 1.740 |
R-factor | 0.1877 |
Rwork | 0.186 |
R-free | 0.22090 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4s2l |
RMSD bond length | 0.018 |
RMSD bond angle | 0.742 |
Data reduction software | MOSFLM |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 62.380 | 1.800 |
High resolution limit [Å] | 1.740 | 1.740 |
Rmerge | 0.037 | 0.410 |
Number of reflections | 25438 | |
<I/σ(I)> | 13.8 | 1.7 |
Completeness [%] | 99.7 | 100 |
Redundancy | 7.1 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2M potassium acetate and 20% w/v PEG 3350 |