2WK1
Structure of the O-methyltransferase NovP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX10.1 |
| Synchrotron site | SRS |
| Beamline | PX10.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-14 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 51.813, 46.038, 61.220 |
| Unit cell angles | 90.00, 104.97, 90.00 |
Refinement procedure
| Resolution | 34.100 - 1.400 |
| R-factor | 0.146 |
| Rwork | 0.145 |
| R-free | 0.16300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vid |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.540 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.300 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.060 | 0.160 |
| Number of reflections | 54638 | |
| <I/σ(I)> | 18.1 | 4.2 |
| Completeness [%] | 98.8 | 89.5 |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 2 M AMMONIUM SULPHATE, 100 MM HEPES BUFFER PH 7.0 |
