5NRI
Crystal structure of Burkholderia pseudomallei D-alanine-D-alanine ligase in complex with AMP and D-Ala-D-Ala
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04-1 |
Synchrotron site | Diamond |
Beamline | I04-1 |
Temperature [K] | 80 |
Detector technology | PIXEL |
Collection date | 2015-02-04 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.917410 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.642, 61.133, 69.972 |
Unit cell angles | 90.00, 90.31, 90.00 |
Refinement procedure
Resolution | 69.970 - 1.500 |
R-factor | 0.13616 |
Rwork | 0.133 |
R-free | 0.20767 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | see publication |
RMSD bond length | 0.027 |
RMSD bond angle | 2.583 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 69.970 |
High resolution limit [Å] | 1.500 |
Number of reflections | 90609 |
<I/σ(I)> | 10.5 |
Completeness [%] | 96.6 |
Redundancy | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | 0.05 to 0.3 M Li2SO4, 0.1 M Bis-Tris pH 5.5 and 15-30% (w/v) PEG 3350, ratio protein:reservoir 1:1 |