3EK2
Crystal structure of eonyl-(acyl carrier protein) reductase from burkholderia pseudomallei 1719b
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-08-01 |
Detector | MAR 300 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.195, 122.195, 139.255 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 69.673 - 1.900 |
R-factor | 0.178 |
Rwork | 0.176 |
R-free | 0.21800 |
Structure solution method | MR, MR |
Starting model (for MR) | 1qsg tetramer modified |
RMSD bond length | 0.018 |
RMSD bond angle | 1.507 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0046) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 69.673 | 2.000 |
High resolution limit [Å] | 1.800 | 1.900 |
Rmerge | 0.142 | 0.598 |
Number of reflections | 82541 | |
<I/σ(I)> | 3.7 | 1 |
Completeness [%] | 95.5 | 97.7 |
Redundancy | 4.7 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 298 | JCSG+ SCREEN: 10% PEG 6000, 100MM HEPES PH 7.0, VAPOR DIFFUSION, TEMPERATURE 298K, pH 7.00, VAPOR DIFFUSION, SITTING DROP |