5F0V
X-ray crystal structure of a thiolase from Escherichia coli at 1.8 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2014-10-13 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.54 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 190.930, 75.310, 147.410 |
| Unit cell angles | 90.00, 131.42, 90.00 |
Refinement procedure
| Resolution | 35.600 - 1.800 |
| R-factor | 0.162 |
| Rwork | 0.160 |
| R-free | 0.19537 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4e1l |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.802 |
| Data reduction software | SCALA (2.2.1) |
| Data scaling software | SCALA (2.2.1) |
| Phasing software | PHASER (2.2.21) |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 35.600 |
| High resolution limit [Å] | 1.800 |
| Rmerge | 0.140 |
| Number of reflections | 135774 |
| <I/σ(I)> | 4.3 |
| Completeness [%] | 99.0 |
| Redundancy | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 295 | 0.2 M Ammonium fluride 20% (w/v) PEG3350 |
