3E2F
Crystal structure of mouse kynurenine aminotransferase III, PLP-bound form
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 | 91.820, 91.820, 233.649 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.210 - 2.590 |
R-factor | 0.19585 |
Rwork | 0.193 |
R-free | 0.24643 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zjg |
RMSD bond length | 0.025 |
RMSD bond angle | 2.211 |
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 | 2.690 |
High resolution limit [Å] | 2.590 | 2.590 |
Rmerge | 0.150 | 0.520 |
Number of reflections | 29301 | |
Completeness [%] | 91.1 | |
Redundancy | 10.4 | 2 |
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 |