4AO9
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 | 88.740, 100.110, 104.799 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.420 - 1.500 |
| R-factor | 0.16766 |
| Rwork | 0.167 |
| R-free | 0.18229 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MES_BFAT_HOLO |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.210 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER (FOR MR) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.420 | 1.580 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.040 | 0.140 |
| Number of reflections | 148964 | |
| <I/σ(I)> | 21.9 | 9.3 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 4.8 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
