3II9
Crystal structure of glutaryl-coa dehydrogenase from Burkholderia pseudomallei at 1.73 Angstrom
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-07-12 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 80.966, 141.268, 84.012 |
| Unit cell angles | 90.00, 112.26, 90.00 |
Refinement procedure
| Resolution | 40.230 - 1.740 |
| R-factor | 0.17164 |
| Rwork | 0.170 |
| R-free | 0.19561 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3d6b |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.159 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.790 |
| High resolution limit [Å] | 1.730 | 1.730 |
| Rmerge | 0.045 | 0.974 |
| Number of reflections | 177485 | |
| <I/σ(I)> | 1.7 | |
| Completeness [%] | 99.3 | 98.6 |
| Redundancy | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microfluidic microbatch | 8.5 | 296 | 19.4% PEG 400, 43 mM Tris 8.5, 86 mM MgCl2, Microfluidic microbatch, temperature 296K |
