1PX6
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 105 |
Detector technology | IMAGE PLATE |
Collection date | 2001-03-15 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54179 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 69.210, 78.760, 89.330 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.100 |
R-factor | 0.19 |
Rwork | 0.190 |
R-free | 0.23500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 11gs |
RMSD bond length | 0.006 |
RMSD bond angle | 1.000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.170 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.103 | 0.479 |
Number of reflections | 28189 | |
<I/σ(I)> | 13.5 | 2.8 |
Completeness [%] | 97.0 | 94.4 |
Redundancy | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 295 | MES, PEG 8000, CALCIUM CHLORIDE, DTT(DITHIOTHREITOL), GLUTATHIONE(REDUCED), pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |