5TXT
Structure of asymmetric apo/holo ALAS dimer from S. cerevisiae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-03-16 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 |
| Unit cell lengths | 63.489, 113.814, 119.344 |
| Unit cell angles | 116.52, 98.18, 92.56 |
Refinement procedure
| Resolution | 35.003 - 2.700 |
| R-factor | 0.1873 |
| Rwork | 0.186 |
| R-free | 0.23180 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5-aminolevulinate synthase |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.636 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.750 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.141 | 0.641 |
| Number of reflections | 80317 | |
| <I/σ(I)> | 13.06 | 2.65 |
| Completeness [%] | 98.8 | 98.2 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 0.1M tri-sodium citrate pH 5.5, 20% PEG 3000 |
