3KUW
Structural basis of the activity ans substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with Fluoro-acetate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9795 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 62.504, 92.896, 49.594 |
Unit cell angles | 90.00, 100.93, 90.00 |
Refinement procedure
Resolution | 38.450 - 1.900 |
R-factor | 0.18866 |
Rwork | 0.185 |
R-free | 0.25572 |
Starting model (for MR) | 1hnn |
RMSD bond length | 0.024 |
RMSD bond angle | 1.904 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.680 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 21719 | |
Completeness [%] | 99.0 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | This-HCl, Fluoroacetate, PEG4000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |