4AOA
Biochemical properties and crystal structure of a novel beta- phenylalanine aminotransferase from Variovorax paradoxus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-07-27 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 88.670, 99.880, 104.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 72.300 - 2.280 |
| R-factor | 0.18422 |
| Rwork | 0.182 |
| R-free | 0.22476 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CBF3 HOLO ENZYME STRUCTURE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.105 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 66.310 | 2.400 |
| High resolution limit [Å] | 2.280 | 2.280 |
| Rmerge | 0.100 | 0.160 |
| Number of reflections | 43283 | |
| <I/σ(I)> | 10.9 | 7.5 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
