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) |