2VEK
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 | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-12-14 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.960, 87.220, 56.480 |
Unit cell angles | 90.00, 97.50, 90.00 |
Refinement procedure
Resolution | 19.740 - 1.600 |
R-factor | 0.167 |
Rwork | 0.166 |
R-free | 0.19300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dkw |
RMSD bond length | 0.015 |
RMSD bond angle | 1.437 |
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 | 1.700 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.120 | 0.410 |
Number of reflections | 56766 | |
<I/σ(I)> | 9.99 | 3.27 |
Completeness [%] | 97.6 | 96.9 |
Redundancy | 4.2 | 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 |