2YII
Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution
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 |
| Collection date | 2009-09-25 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 99.454, 145.999, 99.680 |
| Unit cell angles | 90.00, 99.51, 90.00 |
Refinement procedure
| Resolution | 98.310 - 2.180 |
| R-factor | 0.18053 |
| Rwork | 0.179 |
| R-free | 0.21450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1W27 AND 1Y2M |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.078 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.670 | 2.300 |
| High resolution limit [Å] | 2.180 | 2.180 |
| Rmerge | 0.060 | 0.350 |
| Number of reflections | 142853 | |
| <I/σ(I)> | 2.6 | |
| Completeness [%] | 98.0 | 93.9 |
| Redundancy | 2.1 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4% TACSIMATE PH 6.0, 12% W/V PEG 3350. |
