6AO6
Crystal structure of H108A peptidylglycine alpha-hydroxylating monooxygenase (PHM)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CMOS |
| Collection date | 2013-08-21 |
| Detector | RDI CMOS_8M |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.123, 69.845, 81.992 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 53.170 - 2.980 |
| R-factor | 0.1836 |
| Rwork | 0.180 |
| R-free | 0.26060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1phm |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.463 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.1.29) |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 53.170 | 28.980 | 2.780 |
| High resolution limit [Å] | 2.650 | 8.790 | 2.650 |
| Rmerge | 0.076 | 0.030 | 0.907 |
| Rmeas | 0.093 | 0.038 | 1.107 |
| Rpim | 0.052 | 0.022 | 0.623 |
| Total number of observations | 25247 | 677 | 2737 |
| Number of reflections | 9451 | 267 | 1089 |
| <I/σ(I)> | 10.1 | 27.5 | 1.1 |
| Completeness [%] | 79.0 | 71.8 | 69.3 |
| Redundancy | 2.7 | 2.5 | 2.5 |
| CC(1/2) | 0.996 | 0.997 | 0.428 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8.5 | 293 | 19-24% PEG 4000, Tris HCL |
