5DJ1
Structure of the PLP-Dependent L-Arginine Hydroxylase MppP Holoenzyme
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.98178 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 85.718, 108.277, 195.412 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.450 - 2.102 |
| R-factor | 0.1449 |
| Rwork | 0.144 |
| R-free | 0.17110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Streptomyces globisporus MppP |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.059 |
| Data reduction software | HKL-2000 (705) |
| Data scaling software | HKL-2000 (705) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2148: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.450 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.106 | 0.734 |
| Number of reflections | 106188 | |
| <I/σ(I)> | 30.7 | 5.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 14.4 | 11.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 30% PEG 550 MMe, 50mM MgCl2, 100mM HEPES pH 8.0 |






