2V27
Structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 40.280, 86.020, 87.570 |
| Unit cell angles | 90.00, 97.01, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.500 |
| R-factor | 0.164 |
| Rwork | 0.162 |
| R-free | 0.19500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ltv |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.675 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 1.580 |
| High resolution limit [Å] | 1.600 | 1.500 |
| Rmerge | 0.070 | 0.460 |
| Number of reflections | 94151 | |
| <I/σ(I)> | 12.7 | 2.7 |
| Completeness [%] | 99.6 | 87.5 |
| Redundancy | 4.2 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 1.6-1.8 M AMMONIUM SULFATE, 100 MM NACL, 20 MM NAHEPESPH 7.5 |
