3MOS
The structure of human Transketolase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-05-26 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 113.630, 85.330, 72.740 |
| Unit cell angles | 90.00, 125.69, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.750 |
| R-factor | 0.164 |
| Rwork | 0.162 |
| R-free | 0.20600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qgd |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.995 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.1.1) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.850 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.050 | 0.394 |
| Number of reflections | 55932 | 8396 |
| <I/σ(I)> | 14.78 | 2.8 |
| Completeness [%] | 98.0 | 96.2 |
| Redundancy | 2.5 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.9 | 298 | Crystallization trials revealed a reservoir mixture of 13.5-15 % PEG 6000 (w/v), 4% PEG 400 (v/v) and 2% glycerol (v/v) in 50 mM glycyl-glycine (pH 7.9) optimal for reproducible crystallization of single crystals. To induce crystallization 3 l protein solution (8-12 mg/ml, 0.6 mM ThDP, 5 mM CaCl2 in 50 mM glycyl-glycine (pH 7.9)) were mixed with 3 l of the reservoir solution at room temperature. , VAPOR DIFFUSION, HANGING DROP, temperature 298K |
