3KX8
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 79.910, 71.079, 104.351 |
| Unit cell angles | 90.00, 102.62, 90.00 |
Refinement procedure
| Resolution | 49.750 - 2.350 |
| R-factor | 0.19223 |
| Rwork | 0.190 |
| R-free | 0.24255 |
| Starting model (for MR) | 1hnn |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.568 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.450 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Number of reflections | 47256 | |
| Completeness [%] | 100.0 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Tris HCl PEG 2000mme, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
