3ZU4
Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT172
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 | 101.840, 101.840, 84.750 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 88.200 - 2.010 |
R-factor | 0.17809 |
Rwork | 0.176 |
R-free | 0.22058 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.014 |
RMSD bond angle | 1.471 |
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] | 44.100 | |
High resolution limit [Å] | 2.000 | |
Rmerge | 0.070 | 0.460 |
Number of reflections | 34293 | |
<I/σ(I)> | 14.2 | 3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.4 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 35% PEG 4000, 150 MM AMMONIUM SULFATE, 100 MM MES PH 5.5. |