2VEM
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 | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.800, 86.900, 56.400 |
| Unit cell angles | 90.00, 97.20, 90.00 |
Refinement procedure
| Resolution | 19.660 - 2.200 |
| R-factor | 0.196 |
| Rwork | 0.193 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dkw |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.405 |
| 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 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.140 | 0.620 |
| Number of reflections | 22262 | |
| <I/σ(I)> | 14.36 | 3.63 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 7.6 | 7.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5 |
