3TQX
Structure of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) from Coxiella burnetii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4C |
| Synchrotron site | NSLS |
| Beamline | X4C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-29 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 113.820, 114.850, 136.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.368 - 2.304 |
| R-factor | 0.2184 |
| Rwork | 0.215 |
| R-free | 0.26710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fc4 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.606 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.7.1_743) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 6.230 | 2.300 |
| Rmerge | 0.106 | 0.056 | 0.425 |
| Number of reflections | 38908 | ||
| <I/σ(I)> | 6.7 | ||
| Completeness [%] | 98.1 | 99.7 | 95.2 |
| Redundancy | 3.6 | 3.8 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 295 | 0.1M MES pH 5.0, 20% PEG6000, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
