4ZFA
Cytochrome P450 wild type from BM3 with bound PEG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-10-31 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.9792 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 55.503, 55.503, 717.749 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 59.812 - 2.765 |
R-factor | 0.2466 |
Rwork | 0.244 |
R-free | 0.30170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3npl |
RMSD bond length | 0.002 |
RMSD bond angle | 0.689 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 179.440 | 2.910 |
High resolution limit [Å] | 2.760 | 2.760 |
Rmerge | 0.077 | 0.435 |
Number of reflections | 18145 | |
<I/σ(I)> | 16.2 | 2.3 |
Completeness [%] | 97.0 | 80.2 |
Redundancy | 7.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 17.5mM NiCl2, 50mM PEG MME 2000 |