2QLR
Crystal structure of human kynurenine aminotransferase II
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 | 2007-06-12 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0809 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 109.505, 70.975, 121.133 |
Unit cell angles | 90.00, 101.10, 90.00 |
Refinement procedure
Resolution | 30.110 - 2.300 |
R-factor | 0.24295 |
Rwork | 0.242 |
R-free | 0.25601 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1x0m |
RMSD bond length | 0.022 |
RMSD bond angle | 1.982 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.110 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.119 | 0.422 |
Number of reflections | 96642 | |
Completeness [%] | 92.2 | 75.8 |
Redundancy | 3.9 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 100 mM HEPES, 15% PEG 10000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |