4PB5
D-threo-3-hydroxyaspartate dehydratase H351A mutant complexed with L-erythro-3-hydroxyaspartate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
Synchrotron site | Photon Factory |
Beamline | AR-NW12A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-02-16 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.000 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 157.630, 157.630, 157.537 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.460 - 1.900 |
R-factor | 0.15834 |
Rwork | 0.157 |
R-free | 0.18272 |
RMSD bond length | 0.025 |
RMSD bond angle | 2.116 |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.087 | 0.585 |
Number of reflections | 77555 | |
<I/σ(I)> | 32.12 | 7 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.8 | 14.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | PEG3350, Tris-HCl. MgCl2 |