3PD6
Crystal structure of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV
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 | 2007-11-13 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0809 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 282.393, 78.107, 87.513 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.540 - 2.400 |
R-factor | 0.17751 |
Rwork | 0.177 |
R-free | 0.18937 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hlm |
RMSD bond length | 0.019 |
RMSD bond angle | 1.725 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.130 | 0.340 |
Number of reflections | 76708 | |
Redundancy | 8.1 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 20% PEG 4000, 100mM ammonium sulphate, 6% Glycerol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |