3TQT
Structure of the D-alanine-D-alanine ligase 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 | 2011-02-24 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.238, 97.442, 106.563 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.652 - 1.880 |
| R-factor | 0.1826 |
| Rwork | 0.180 |
| R-free | 0.22370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.055 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.930 |
| High resolution limit [Å] | 1.880 | 5.160 | 1.880 |
| Rmerge | 0.043 | 0.028 | 0.379 |
| Number of reflections | 56853 | ||
| <I/σ(I)> | 13.6 | ||
| Completeness [%] | 97.9 | 93.3 | 94.9 |
| Redundancy | 4.7 | 4.7 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | sitting drop | 6 | 293 | 100 mM MES pH 6.0, 5% PEG 3350, 30% PEG 200, sitting drop, temperature 293K |
