2HXP
Crystal Structure of the human phosphatase (DUSP9)
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-30 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.1, 1.7 |
Spacegroup name | P 32 |
Unit cell lengths | 50.527, 50.527, 59.851 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.700 - 1.830 |
R-factor | 0.216 |
Rwork | 0.216 |
R-free | 0.24600 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.700 | 1.900 |
High resolution limit [Å] | 1.830 | 1.830 |
Rmerge | 0.022 | 0.140 |
Number of reflections | 14920 | |
<I/σ(I)> | 47.1 | 19 |
Completeness [%] | 99.2 | 100 |
Redundancy | 11.4 | 10 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 25% PEG 3350, 0.1M Bis-Tris, 0.2M Ammonium Sulphate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |