1WNU
Structure of Archaeal Trans-Editing Protein AlaX in complex with L-serine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-12-11 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 33.968, 88.472, 109.921 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.800 |
Rwork | 0.228 |
R-free | 0.26560 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1v7o |
RMSD bond length | 0.008 |
RMSD bond angle | 1.345 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 8871 | |
<I/σ(I)> | 11.7 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 8.8 | 8.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.6 | 293 | PEG4000, MPD, Tris, pH 8.6, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |