1I45
YEAST TRIOSEPHOSPHATE ISOMERASE (MUTANT)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-05-10 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 60.601, 97.058, 49.245 |
| Unit cell angles | 90.00, 91.70, 90.00 |
Refinement procedure
| Resolution | 29.750 - 1.800 |
| R-factor | 0.175 |
| Rwork | 0.175 |
| R-free | 0.20800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ypi |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.200 |
| Data scaling software | SCALEPACK |
| Phasing software | COMO |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.073 * | 0.305 |
| Total number of observations | 152637 * | |
| Number of reflections | 50459 * | |
| <I/σ(I)> | 44.2 | |
| Completeness [%] | 95.2 | 82.4 |
| Redundancy | 2.9 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 6.8 | 293 | 16% PEG 4000, 50mM Tris, 50mM NaCl, pH 6.8, batch at 293 K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 40 (mg/ml) | |
| 2 | 1 | 1 | Tris-HCl | 50 (mM) | |
| 3 | 1 | 1 | 50 (mM) | ||
| 4 | 1 | 1 | EDTA | 1 (mM) | pH6.8 |
| 5 | 1 | 1 | PEG4000 | 14-16 (%) |
