4PB3
D-threo-3-hydroxyaspartate dehydratase H351A mutant
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) | 1.0000 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 157.603, 157.603, 157.426 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.700 |
R-factor | 0.1668 |
Rwork | 0.166 |
R-free | 0.18514 |
RMSD bond length | 0.026 |
RMSD bond angle | 2.349 |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.730 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.059 | 0.464 |
Number of reflections | 107707 | |
<I/σ(I)> | 38.3 | 5.44 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.1 | 8.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | PEG3350, Tris-HCl, MgCl2 |