2VVM
The structure of MAO-N-D5, a variant of monoamine oxidase from Aspergillus niger.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-09-20 |
| Detector | ADSC CCD |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 107.419, 107.419, 235.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 97.590 - 1.850 |
| R-factor | 0.182 |
| Rwork | 0.181 |
| R-free | 0.20500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SELENOMET STRUCTURE OF MONOAMINE OXIDASE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.276 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.4.0065) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.090 | 0.660 |
| Number of reflections | 66613 | |
| <I/σ(I)> | 28.2 | 1.8 |
| Completeness [%] | 99.8 | 98.5 |
| Redundancy | 17.2 | 8.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 10% PEG 3350, 0.2M PROLINE, 0.1M HEPES PH7.5 |
