2VEL
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 | 44.820, 85.600, 55.270 |
Unit cell angles | 90.00, 98.23, 90.00 |
Refinement procedure
Resolution | 19.930 - 2.300 |
R-factor | 0.184 |
Rwork | 0.180 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dkw |
RMSD bond length | 0.012 |
RMSD bond angle | 1.427 |
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 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.150 | 0.540 |
Number of reflections | 18376 | |
<I/σ(I)> | 10.71 | 3 |
Completeness [%] | 99.7 | 100 |
Redundancy | 4.3 | 4.3 |
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 |