5UU6
The crystal structure of nitroreductase A from Vibrio parahaemolyticus RIMD 2210633
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 | PIXEL |
| Collection date | 2017-02-08 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97919 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.004, 71.609, 110.450 |
| Unit cell angles | 90.00, 93.15, 90.00 |
Refinement procedure
| Resolution | 43.689 - 1.950 |
| R-factor | 0.1652 |
| Rwork | 0.163 |
| R-free | 0.20980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bkj |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.155 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX ((1.11.1_2575)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.104 | 0.819 |
| Rpim | 0.067 | 0.572 |
| Number of reflections | 64115 | 3042 |
| <I/σ(I)> | 10.3 | 1.82 |
| Completeness [%] | 98.2 | 93.1 |
| Redundancy | 3.2 | 2.5 |
| CC(1/2) | 0.593 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | 0.2 M Magnesium Chloride, 0.1 M Bis-Tris:HCl, 25% (w/v) PEG 3350 |
