2DU8
Crystal structure of human D-amino acid oxidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-05-24 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 150.976, 183.184, 51.075 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.780 - 2.500 |
R-factor | 0.22535 |
Rwork | 0.223 |
R-free | 0.27006 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1an9 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.384 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 116.250 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.077 | 0.377 |
Number of reflections | 49644 | |
<I/σ(I)> | 13.4 | |
Completeness [%] | 99.5 | 99.8 |
Redundancy | 5.8 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 288 | 10% PEG 4000, 0.2M ammonium acetate, 0.1M sodium citrate, 12% glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 288.0K |