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 |