2VEI
Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR591 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-05-13 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 91.240, 52.590, 92.380 |
| Unit cell angles | 90.00, 119.04, 90.00 |
Refinement procedure
| Resolution | 18.850 - 1.890 |
| R-factor | 0.168 |
| Rwork | 0.166 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dkw |
| RMSD bond length | 0.012 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0028) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.950 |
| High resolution limit [Å] | 1.890 | 1.890 |
| Rmerge | 0.060 | 0.150 |
| Number of reflections | 61427 | |
| <I/σ(I)> | 18.4 | 7.32 |
| Completeness [%] | 99.3 | 99.7 |
| Redundancy | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 0.1 M TRIS/HCL PH 8.5, 1.9 M MGSO4 |
