4EGJ
Crystal structure of D-alanine-D-alanine ligase from Burkholderia xenovorans
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-02-22 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 |
Unit cell lengths | 78.930, 78.930, 224.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.990 - 2.300 |
R-factor | 0.2254 |
Rwork | 0.224 |
R-free | 0.25970 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3eg0 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.698 |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.360 | |
High resolution limit [Å] | 2.300 | 10.290 | 2.300 |
Rmerge | 0.078 | 0.017 | 0.478 |
Number of reflections | 59426 | 602 | 4433 |
<I/σ(I)> | 10.11 | 28.36 | 2.09 |
Completeness [%] | 97.8 | 84.4 | 99.3 |
Redundancy | 2.5 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | Qiagen JCSG Core1 screen d5: 20% PEG 3350, 200mM LiCl; BuxeA.00119.a.A1 PS01358 at 23.2mg/ml, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K |