6MI0
Crystal structure of the P450 domain of the CYP51-ferredoxin fusion protein from Methylococcus capsulatus, ligand-free state
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-05-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 151.861, 151.861, 67.246 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 65.840 - 2.730 |
| R-factor | 0.21502 |
| Rwork | 0.214 |
| R-free | 0.23426 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6mcw |
| RMSD bond length | 0.002 |
| RMSD bond angle | 1.103 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.840 | 2.800 |
| High resolution limit [Å] | 2.730 | 2.730 |
| Rmerge | 0.055 | 0.800 |
| Number of reflections | 24087 | 3463 |
| <I/σ(I)> | 16 | 1.2 |
| Completeness [%] | 97.6 | 99.9 |
| Redundancy | 5.3 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 291 | Potassium phosphate, PEG 3350, glycerol |
