3FHX
Crystal structure of D235A mutant of human pyridoxal kinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2008-04-11 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54178 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 91.224, 115.422, 168.898 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.930 - 2.500 |
R-factor | 0.214 |
Rwork | 0.212 |
R-free | 0.26200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yxu |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 32.690 | 32.690 | 2.590 |
High resolution limit [Å] | 2.500 | 5.380 | 2.500 |
Rmerge | 0.083 | 0.035 | 0.298 |
Total number of observations | 13989 | 13462 | |
Number of reflections | 31128 | ||
<I/σ(I)> | 26.3 | 4.2 | |
Completeness [%] | 99.7 | 98.8 | 99.6 |
Redundancy | 3.99 | 4.05 | 3.79 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | Protein solution: 20 mM Sodium BES buffer pH 7.2, 100 mM NaCl, 5 mM BME, 2.5 mM MgATP, 1 mM PLP. Precipitant: 100 mM Tris-HCl pH 8.0, 57% MPD, 5 mM MgSO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K |