3KGG
X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): Perdeuteration of proteins for neutron diffraction
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | CCD |
Collection date | 2007-07-01 |
Detector | RIGAKU SATURN 92 |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.140, 83.150, 87.440 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 500.000 - 2.100 |
R-factor | 0.1764 |
Rwork | 0.176 |
R-free | 0.21750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2GVW.pdb |
RMSD bond length | 0.006 |
RMSD bond angle | 1.431 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 500.000 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.577 | |
Number of reflections | 18978 | |
<I/σ(I)> | 2.9 | |
Completeness [%] | 99.8 | 100 |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 11 % PEG 6000, RT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |