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 |