4EC3
Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-21 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.8104 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 98.763, 92.943, 63.579 |
| Unit cell angles | 90.00, 100.31, 90.00 |
Refinement procedure
| Resolution | 43.190 - 2.650 |
| R-factor | 0.183 |
| Rwork | 0.180 |
| R-free | 0.23520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3d2h |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.873 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.200 | 2.750 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Number of reflections | 16229 | |
| <I/σ(I)> | 9.7 | 2.7 |
| Completeness [%] | 98.2 | 97.9 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 0.2 M MgCl2, 30% (w/v) polyethylene glycol 4,000, 0.1 M Tris/HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
