3EOM
2.4 A crystal structure of native glutaryl-coa dehydrogenase from Burkholderia pseudomallei
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-01-01 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 98.115, 106.768, 145.425 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.398 |
R-factor | 0.213 |
Rwork | 0.211 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.262 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.490 |
High resolution limit [Å] | 2.398 | 5.170 | 2.398 |
Rmerge | 0.084 | 0.057 | 0.658 |
Number of reflections | 60203 | ||
<I/σ(I)> | 23.7 | ||
Completeness [%] | 99.5 | 99.1 | 98.2 |
Redundancy | 7 | 6.7 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 289 | 20% PEG 3000, 0.1M HEPES pH 7.5, 0.2M NaCl, VAPOR DIFFUSION, temperature 289K |