1QG6
CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 300 |
| Detector technology | CCD |
| Collection date | 1998-09-01 |
| Detector | ADSC |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.160, 80.290, 82.750 |
| Unit cell angles | 90.00, 104.46, 90.00 |
Refinement procedure
| Resolution | 100.000 - 1.900 |
| R-factor | 0.201 * |
| Rwork | 0.202 |
| R-free | 0.20700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dfh |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.400 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (98.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.450 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.099 | 0.406 |
| Total number of observations | 92854 * | |
| Number of reflections | 57294 | 4320 * |
| <I/σ(I)> | 4.2 | 1.2 |
| Completeness [%] | 78.2 * | 40.6 * |
| Redundancy | 1.6 | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5 | HANGING DROPS WERE FORMED BY MIXING 4MICROLITRES OF COMPLEX SOLUTION (15MG/ML PROTEIN, 3MM NADH, 0.6MM TRICLOSAN) WITH 4 MICROLITRES OF A RESERVOIR SOLUTION CONTAINING 12-16% (W/V) PEG 400 AND 0.1M SODIUM ACETATE PH 4.8-5.2 AT ROOM TEMPERATURE, pH 5.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | drop | NADH | 3 (mM) | |
| 3 | 1 | drop | triclosan | 0.6 (mM) | |
| 4 | 1 | reservoir | PEG400 | 12-16 (%(w/v)) | |
| 5 | 1 | reservoir | sodium acetate | 0.1 (M) |
