3B7K
Human Acyl-coenzyme A thioesterase 12
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-11-10 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.93400 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 82.700, 126.050, 185.340 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.890 - 2.700 |
| R-factor | 0.2362 |
| Rwork | 0.234 |
| R-free | 0.28479 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vpm |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.110 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0040) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.116 | 0.598 |
| Number of reflections | 26807 | |
| <I/σ(I)> | 12.5 | 3.37 |
| Completeness [%] | 99.3 | 100 |
| Redundancy | 7.16 | 7.33 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 350mM NaSCN, 25% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
