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 |