4PZF
Berberine bridge enzyme G164A variant, a reticuline dehydrogenase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-03-10 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.97242 |
| Spacegroup name | P 2 2 21 |
| Unit cell lengths | 80.820, 175.440, 195.810 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.378 - 2.200 |
| R-factor | 0.2209 |
| Rwork | 0.220 |
| R-free | 0.24190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3d2h |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.840 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (mr) |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Number of reflections | 140296 | |
| <I/σ(I)> | 11.78 | 1.63 |
| Completeness [%] | 99.0 | 98.4 |
| Redundancy | 8.2 | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 30mg/mL protein + 0.1 M HEPES pH 7.5, 2.0 M Ammonium sulfate, BATCH, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
