3E2Z
Crystal structure of mouse kynurenine aminotransferase III in complex with kynurenine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-06-27 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0809 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 91.490, 91.490, 233.501 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.640 - 2.810 |
R-factor | 0.19394 |
Rwork | 0.192 |
R-free | 0.23654 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zjg |
RMSD bond length | 0.024 |
RMSD bond angle | 2.205 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.120 | 0.390 |
Number of reflections | 24119 | |
Completeness [%] | 95.6 | |
Redundancy | 11.9 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 21% PEG 400, 150 mM CaCl2, 10% Glycerol, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |