2V28
Apo structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 40.430, 86.290, 87.670 |
| Unit cell angles | 90.00, 96.64, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.950 |
| R-factor | 0.201 |
| Rwork | 0.198 |
| R-free | 0.26500 |
| Structure solution method | OTHER |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.337 |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.110 | 0.510 |
| Number of reflections | 42547 | |
| <I/σ(I)> | 7 | 2.4 |
| Completeness [%] | 97.6 | 96.8 |
| Redundancy | 2.4 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 1.6-1.8 M AMMONIUM SULFATE 100 MM NACL 20 MM NAHEPES PH 7.5 |
