5J8G
Structure of nitroreductase from E. cloacae complexed with para-nitrobenzoic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-ID-B |
| Synchrotron site | APS |
| Beamline | 14-ID-B |
| Temperature [K] | 115 |
| Detector technology | CCD |
| Collection date | 2002-10-10 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.410, 113.440, 82.290 |
| Unit cell angles | 90.00, 101.55, 90.00 |
Refinement procedure
| Resolution | 19.923 - 1.900 |
| R-factor | 0.1696 |
| Rwork | 0.166 |
| R-free | 0.19720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.538 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.923 | 20.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 4.080 | 1.900 |
| Rmerge | 0.064 | 0.270 | |
| Rmeas | 0.077 | 0.323 | |
| Rpim | 0.042 | 0.176 | |
| Completeness [%] | 98.4 | 97.6 | |
| Redundancy | 3.2 | 3.2 | |
| CC(1/2) | 0.990 | 0.885 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 278 | 100 mM homopipes (pH 4.8), 20 mM para-nitrobenzoic acid, and 13% w/v polyethylene glycol 4000. Protein at 4.75 mg/ml initial concentration in 10 mM HEPES (pH 7.0) and 50 mM KCl |
