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 |