2QQ2
Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-07-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.93300 |
| Spacegroup name | P 1 |
| Unit cell lengths | 80.950, 81.600, 105.100 |
| Unit cell angles | 79.61, 89.70, 74.12 |
Refinement procedure
| Resolution | 19.870 - 2.800 |
| R-factor | 0.2171 |
| Rwork | 0.216 |
| R-free | 0.23921 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vpm |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.420 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.3.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.091 | 0.602 |
| Number of reflections | 59646 | |
| <I/σ(I)> | 9.65 | 2.43 |
| Completeness [%] | 95.3 | 97.4 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 0.1M Bis-Tris, 0.2mM MgCl2, 20% PEG 3350, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
