3ZU2
Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)
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 65 2 2 |
Unit cell lengths | 104.160, 104.160, 219.140 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.821 - 2.100 |
R-factor | 0.2009 |
Rwork | 0.199 |
R-free | 0.22790 |
Structure solution method | SIRAS |
Starting model (for MR) | NONE |
RMSD bond length | 0.007 |
RMSD bond angle | 1.136 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | autoSHARP |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.400 | |
High resolution limit [Å] | 2.100 | |
Rmerge | 0.060 | 0.620 |
Number of reflections | 48035 | |
<I/σ(I)> | 15.8 | 3 |
Completeness [%] | 99.8 | 100 |
Redundancy | 7.2 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 1.25M SODIUM MALONATE, 100MM IMIDAZOLE PH 8.25. | |||
1 | 1.25M SODIUM MALONATE, 100MM IMIDAZOLE PH 8.25. |