2ISQ
Crystal Structure of O-Acetylserine Sulfhydrylase from Arabidopsis Thaliana in Complex with C-Terminal Peptide from Arabidopsis Serine Acetyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-15 |
Detector | BRUKER SMART 6000 |
Wavelength(s) | 1.54 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 104.860, 104.860, 99.315 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 2.800 |
Rwork | 0.188 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB 1Z7W |
RMSD bond length | 0.006 |
RMSD bond angle | 1.280 |
Data reduction software | SAINT |
Data scaling software | PROTEUM PLUS (PLUS) |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 19828 | |
<I/σ(I)> | 7.36 | 2.01 |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.8 | 10 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 1.5 M ammonium sulfate; 0.1 M PIPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |