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. |