1MD4
A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-05-03 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.54179 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.270, 89.440, 68.920 |
| Unit cell angles | 90.00, 98.07, 90.00 |
Refinement procedure
| Resolution | 14.990 - 2.100 |
| R-factor | 0.207 |
| Rwork | 0.207 |
| R-free | 0.23600 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 10gs |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.190 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.170 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.117 | 0.518 |
| Total number of observations | 78780 * | |
| Number of reflections | 25365 | |
| <I/σ(I)> | 10.7 | 1.9 |
| Completeness [%] | 93.7 | 79.3 |
| Redundancy | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 22 * | MES, PEG 8000, calcium chloride, DTT(dithiothreitol), glutathione(reduced), pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 4.2 (mg/ml) | |
| 2 | 1 | drop | EDTA | 1 (mM) | |
| 3 | 1 | drop | dithiothreitol | 1 (mM) | |
| 4 | 1 | drop | HEPES | 10 (mM) | pH7.0 |
| 5 | 1 | reservoir | PEG8000 | 15-25 (%(w/v)) | |
| 6 | 1 | reservoir | 20 (mM) | ||
| 7 | 1 | reservoir | GSH | 1 (mM) | |
| 8 | 1 | reservoir | dithiothreitol | 10 (mM) | |
| 9 | 1 | reservoir | MES | 100 (mM) | pH5.2-5.8 |
