3GK0
Crystal structure of pyridoxal phosphate biosynthetic protein from Burkholderia pseudomallei
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-12-03 |
Wavelength(s) | 0.97934 |
Spacegroup name | P 1 |
Unit cell lengths | 90.090, 91.864, 90.024 |
Unit cell angles | 118.48, 116.81, 93.50 |
Refinement procedure
Resolution | 46.500 - 2.280 |
R-factor | 0.189 |
Rwork | 0.186 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m5w |
RMSD bond length | 0.009 |
RMSD bond angle | 1.152 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.280 | 2.280 |
Rmerge | 0.107 | 0.481 |
Number of reflections | 91137 | |
<I/σ(I)> | 12.627 | 2.1 |
Completeness [%] | 96.5 | 85.2 |
Redundancy | 3.7 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 16.4% PEG4000, 0.1 M Hepes NaOH, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |