5ER6
Crystal structure of an 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 | 2015-07-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.010, 94.810, 99.490 |
| Unit cell angles | 90.00, 99.54, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.550 |
| R-factor | 0.1459 |
| Rwork | 0.146 |
| R-free | 0.16700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4gh5 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.767 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX (dev_2219) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 6.930 | 1.590 |
| High resolution limit [Å] | 1.550 | 4.900 | 1.550 |
| Rmerge | 0.078 | 0.042 | 0.526 |
| Rmeas | 0.089 | 0.048 | 0.601 |
| Total number of observations | 576794 | ||
| Number of reflections | 135447 | 2856 | 9845 |
| <I/σ(I)> | 12.18 | 26.61 | 2.88 |
| Completeness [%] | 98.3 | 99.8 | 96.9 |
| Redundancy | 4.26 | 4.29 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 290 | JCSG+ H10: 200mM Ammonium sulfate, 100mM BIS-Tris pH5.5 25% PEG3350; BrovA.00010.a.B1.PS02326 at 24.76mg/Ml; 15% EG; tray 261921h10; puck ixr1-8 |
