2ZJG
Crystal structural of mouse kynurenine aminotransferase III
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2008-01-21 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0908 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 91.090, 91.090, 233.050 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.580 - 3.000 |
R-factor | 0.22217 |
Rwork | 0.222 |
R-free | 0.23258 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1w7l |
RMSD bond length | 0.024 |
RMSD bond angle | 2.049 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | PHASES |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.150 | 0.470 |
Number of reflections | 20485 | |
Completeness [%] | 97.4 | 81.1 |
Redundancy | 12 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 20% PEG2000, 150mM CaCl2, 5% glycerol, 200mM HEPES, pH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |