5HA5
Crystal structure of an NAD-bound oxidoreductase from Brucella ovis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-12-11 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.500, 96.820, 101.900 |
| Unit cell angles | 90.00, 100.75, 90.00 |
Refinement procedure
| Resolution | 48.410 - 1.950 |
| R-factor | 0.1519 |
| Rwork | 0.151 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.897 |
| Data scaling software | XSCALE |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.950 | |
| High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
| Rmerge | 0.070 | 0.017 | 0.480 |
| Rmeas | 0.082 | 0.020 | 0.560 |
| Total number of observations | 296987 | ||
| Number of reflections | 78788 | 916 | 5808 |
| <I/σ(I)> | 15.52 | 50.2 | 2.72 |
| Completeness [%] | 99.9 | 98.6 | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 290 | MORPHEUS H2: 10% PEG8000, 20%EG, 20mM each amino acid, 100mM MES/imidazole pH6.5, 5mM NADP; protein conc. 24.8mg/mL; direct cryo; puck yum7-6 |
