3MIF
Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.10 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.246, 69.715, 83.121 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.630 - 2.000 |
| R-factor | 0.20822 |
| Rwork | 0.207 |
| R-free | 0.23539 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1phm |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.102 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 37462 | |
| <I/σ(I)> | 4.6 | 1.5 |
| Completeness [%] | 97.0 | 100 |
| Redundancy | 5.9 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | Crystallization: 0.1-0.5mM CuSO4, 1.25mM NiCl2, 100mM sodium cacodylate pH=5.5, 3mM sodium azide and 5% glycerol. Then, CO-soaking in a pressure chamber at 3 atm of CO for 15 minutes at RT., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
