5JRO
The crystal structure of azoreductase from Yersinia pestis CO92 in its Apo form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-09-28 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97931 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 124.257, 45.135, 72.699 |
| Unit cell angles | 90.00, 112.84, 90.00 |
Refinement procedure
| Resolution | 33.500 - 2.540 |
| R-factor | 0.202 |
| Rwork | 0.200 |
| R-free | 0.24890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | : 4ESE |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.511 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX ((dev-2386_1692: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.500 | 2.580 |
| High resolution limit [Å] | 2.540 | 2.540 |
| Rmerge | 0.056 | 0.451 |
| Number of reflections | 12240 | |
| <I/σ(I)> | 25.74 | 2.35 |
| Completeness [%] | 96.9 | 81.3 |
| Redundancy | 3.5 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 289 | 0.1M CHES:NaOH, 30% (w/v) PEG 3000 |
