5IHV
Crystal structure of a beta-lactamase from Burkholderia ambifaria
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-11-20 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.260, 63.080, 73.850 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.100 |
R-factor | 0.1372 |
Rwork | 0.137 |
R-free | 0.16680 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3w4q |
RMSD bond length | 0.012 |
RMSD bond angle | 1.285 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX (dev_2328) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.130 | |
High resolution limit [Å] | 1.100 | 4.920 | 1.100 |
Rmerge | 0.049 | 0.027 | 0.496 |
Number of reflections | 92835 | ||
<I/σ(I)> | 18 | 46.18 | 2.18 |
Completeness [%] | 98.8 | 93.5 | 89.4 |
Redundancy | 5.6 | ||
CC(1/2) | 0.999 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 290 | JCSG+ A7 (267021a7): 100mM CHES pH 9.5, 20% PEG8000, protein conc. 48.83mg/mL; cryo 20% EG; puck uqf3-6 |