7R27
Crystal structure of the L. plantarum D-alanine ligase DltA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-06-14 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97856 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 68.522, 53.573, 102.072 |
Unit cell angles | 90.00, 96.78, 90.00 |
Refinement procedure
Resolution | 47.360 - 2.010 |
R-factor | 0.2115 |
Rwork | 0.209 |
R-free | 0.26600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3dhv |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20_4459) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.360 | 2.060 |
High resolution limit [Å] | 2.010 | 2.010 |
Rmerge | 0.171 | 1.452 |
Number of reflections | 49012 | 3478 |
<I/σ(I)> | 7.2 | 0.9 |
Completeness [%] | 99.4 | |
Redundancy | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | PEG3350, KCl |