1MTC
GLUTATHIONE TRANSFERASE MUTANT Y115F
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | SIEMENS |
| Temperature [K] | 143 |
| Detector technology | AREA DETECTOR |
| Collection date | 1995-03-25 |
| Detector | BRUKER |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 86.750, 68.580, 80.460 |
| Unit cell angles | 90.00, 105.12, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gst |
| RMSD bond length | 0.011 |
| RMSD bond angle | 0.039 |
| Data reduction software | X-GEN |
| Data scaling software | X-GEN |
| Phasing software | SHELXS |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 2.260 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.110 | 0.230 |
| Number of reflections | 21775 | |
| <I/σ(I)> | 33 | 8 |
| Completeness [%] | 94.0 | 91 |
| Redundancy | 3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 | Ji, X., (1992) Biochemistry, 31, 10169. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | Tris | 25 (mM) | pH8.0 |
| 3 | 1 | drop | EDTA | 1 (mM) | |
| 4 | 1 | drop | beta-D-glucopyranoside | 0.2 (%) | |
| 5 | 1 | drop | inhibitor | 1 (mM) | pH8. |
| 6 | 1 | drop | ammonium sulfate | 40-50 (%sat) | |
| 7 | 1 | reservoir | ammonium sulfate | 60-72 (%sat) | |
| 8 | 1 | reservoir | Tris | 25 (mM) | pH8.0 |
