1DFH
X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-02-26 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 80.900, 80.900, 328.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.200 |
| Rwork | 0.194 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | E. COLI ENR |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.608 |
| Data reduction software | MOSFLM |
| Data scaling software | Agrovata |
| Phasing software | CCP4 |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.600 | 2.260 |
| High resolution limit [Å] | 2.200 | 2.210 |
| Rmerge | 0.058 | 0.139 |
| Total number of observations | 76176 * | |
| Number of reflections | 31179 | |
| <I/σ(I)> | 8.98 | 5.2 |
| Completeness [%] | 95.0 | 56.6 |
| Redundancy | 2.4 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | Baldock, C., (1996) Acta Crystallogr.,Sect.D, 52, 1181. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | 10 (mM) | ||
| 3 | 1 | drop | dithiothreitol | 1 (mM) | |
| 4 | 1 | drop | NAD+ | 10 (mM) | |
| 5 | 1 | reservoir | PEG400 | 15 (%) | |
| 6 | 1 | reservoir | acetate | 100 (mM) |
