3MIH
Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide, obtained in the presence of substrate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4C |
| Synchrotron site | NSLS |
| Beamline | X4C |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-11-16 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.110, 68.800, 79.791 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 52.000 - 2.740 |
| R-factor | 0.23994 |
| Rwork | 0.237 |
| R-free | 0.29587 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1phm |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.967 |
| 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] | 52.000 | 2.850 |
| High resolution limit [Å] | 2.740 | 2.750 |
| Number of reflections | 8970 | |
| <I/σ(I)> | 21.1 | 1.7 |
| Completeness [%] | 87.3 | 49.3 |
| Redundancy | 4.8 | 3 |
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. The crystal was first soaked in 1mM substrate (Ac-3,5-diI-YG) for 1 hour and then soaked in 40mM NaN3/1mM substrate for 8 hours at 293K., VAPOR DIFFUSION, HANGING DROP |
