4ESE
The crystal structure of azoreductase from Yersinia pestis CO92 in complex with FMN.
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 | 2012-04-09 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97934 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 51.825, 120.388, 60.074 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.403 - 1.450 |
| R-factor | 0.1753 |
| Rwork | 0.174 |
| R-free | 0.20000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1t5b |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.057 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.000 | 1.480 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.057 | 0.592 |
| Number of reflections | 33841 | |
| <I/σ(I)> | 38.5 | 2.2 |
| Completeness [%] | 99.8 | 99.6 |
| Redundancy | 5.1 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 15% (w/v) PEG1500, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
