5TXR
Structure of ALAS from S. cerevisiae non-covalently bound to PLP cofactor
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 21 1 |
| Unit cell lengths | 78.613, 64.878, 95.693 |
| Unit cell angles | 90.00, 95.86, 90.00 |
Refinement procedure
| Resolution | 22.727 - 1.900 |
| R-factor | 0.1424 |
| Rwork | 0.142 |
| R-free | 0.17210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | R. capsulatus ALAS |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.673 |
| 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 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 73470 | |
| <I/σ(I)> | 13.24 | 1.24 |
| Completeness [%] | 96.6 | 98.2 |
| Redundancy | 5.1 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.2M Potassium formate, 20% PEG 3350 |
