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 |