3ZU5
Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT173
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS HTC |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 101.770, 101.770, 84.550 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.120 - 2.000 |
| R-factor | 0.18941 |
| Rwork | 0.187 |
| R-free | 0.22839 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.510 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.200 | |
| High resolution limit [Å] | 2.000 | |
| Rmerge | 0.080 | 0.540 |
| Number of reflections | 34559 | |
| <I/σ(I)> | 13.1 | 2.5 |
| Completeness [%] | 100.0 | 1 |
| Redundancy | 5.9 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 37% PEG 4000, 150 MM AMMONIUM SULFATE, 100 MM MES PH 5.5. |
