1C14
CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS |
| Synchrotron site | APS |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-01-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 79.000, 79.000, 328.750 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 7.000 - 2.000 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.26300 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 23.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.063 | 0.265 |
| Total number of observations | 112233 * | |
| Number of reflections | 21505 | |
| <I/σ(I)> | 16 | |
| Completeness [%] | 97.0 | 93 |
| Redundancy | 5.2 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 300 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | HEPES | 0.1 (M) | |
| 3 | 1 | reservoir | ammonium sulfate | 2 (M) | |
| 4 | 1 | reservoir | PEG400 | 5 (%) |
