2CL5
Catechol-O-methyltransferase in complex with an inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.767, 79.627, 61.540 |
| Unit cell angles | 90.00, 91.14, 90.00 |
Refinement procedure
| Resolution | 62.020 - 1.600 |
| R-factor | 0.151 |
| Rwork | 0.149 |
| R-free | 0.17800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h1d |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.740 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.420 | 1.640 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.050 | 0.400 |
| Number of reflections | 67299 | |
| <I/σ(I)> | 21.6 | 3.2 |
| Completeness [%] | 99.9 | 98.2 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 8% PEG6K, 0.1 M MES PH 6.0 |
