3UPL
Crystal structure of the Brucella abortus enzyme catalyzing the first committed step of the methylerythritol 4-phosphate pathway.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-02-20 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.8726 |
Spacegroup name | P 1 |
Unit cell lengths | 49.365, 63.380, 79.123 |
Unit cell angles | 68.63, 75.80, 72.70 |
Refinement procedure
Resolution | 25.000 - 1.500 |
R-factor | 0.1514 |
Rwork | 0.150 |
R-free | 0.17630 |
Structure solution method | SAD |
RMSD bond length | 0.022 |
RMSD bond angle | 1.964 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.044 | 0.200 |
Number of reflections | 129797 | |
<I/σ(I)> | 28.8 | 4.7 |
Completeness [%] | 96.8 | 92.5 |
Redundancy | 2.9 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 14-20% PEG4000, 0.1M HEPES, 0.2M magnesium chloride, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |