2Q2B
Crystal structure of the C-terminal domain of mouse acyl-CoA thioesterase 7
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-10-06 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 136.743, 136.743, 99.833 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.390 - 2.500 |
| R-factor | 0.22516 |
| Rwork | 0.222 |
| R-free | 0.28780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vpm |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.375 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.400 | 2.570 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.051 | 0.520 |
| Number of reflections | 11896 | |
| <I/σ(I)> | 18.3 | 2.1 |
| Redundancy | 2.3 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 290 | 20-30%PEG 3350, 0.1M Tris, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
