4V1Y
The structure of the hexameric atrazine chlorohydrolase, AtzA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-05-10 |
Detector | ADSC CCD |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 117.487, 195.564, 283.882 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 161.050 - 2.800 |
R-factor | 0.1889 |
Rwork | 0.187 |
R-free | 0.21794 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hpa |
RMSD bond length | 0.014 |
RMSD bond angle | 1.505 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.500 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.230 | 0.910 |
Number of reflections | 161122 | |
<I/σ(I)> | 8.8 | 2.6 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.5 | 7.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.1 | THE PROTEIN WAS CONCENTRATED TO 11.4 MG/ML AND SET UP IN A 1:1 RATIO, 150 NL PLUS 150 NL, WITH 50 MM HEPES PH 7.1, 2.7% DIETHYLENE GLYCOL, 5.5% PEG 8000 |