5EGJ
The structural and biochemical characterization of acyl-coa hydrolase mutant Asn28Ala from Staphylococcus aureus in complex with COENZYME A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-31 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 127.730, 127.730, 55.722 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.440 - 2.400 |
| R-factor | 0.21 |
| Rwork | 0.207 |
| R-free | 0.25710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ncp |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.041 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_1894) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.440 | 2.486 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.029 | 0.098 |
| Number of reflections | 10919 | |
| <I/σ(I)> | 8.73 | 3.61 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 296 | 0.1M Sodium HEPES pH7.5, 0.8 M Sodium phosphate monobasic |
