3ZU3
Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (MR, cleaved Histag)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 102.160, 102.160, 84.761 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.616 - 1.802 |
| R-factor | 0.1702 |
| Rwork | 0.168 |
| R-free | 0.21240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zu2 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.074 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.400 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.110 | 0.630 |
| Number of reflections | 47522 | |
| <I/σ(I)> | 13.2 | 3.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.4 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 25% PEG 4000, 150 MM AMMONIUM SULFATE 100 MM, MES PH 5.5. |
