2VEN
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 | 46.100, 88.300, 56.500 |
Unit cell angles | 90.00, 97.00, 90.00 |
Refinement procedure
Resolution | 19.880 - 2.000 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dkw |
RMSD bond length | 0.015 |
RMSD bond angle | 1.450 |
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 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.170 | 0.640 |
Number of reflections | 30031 | |
<I/σ(I)> | 11.51 | 3.47 |
Completeness [%] | 98.8 | 98.4 |
Redundancy | 5.3 | 5.4 |
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 |