3KU9
X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Detector technology | CCD |
Collection date | 2009-04-24 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 138.957, 138.957, 189.800 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 3.200 |
R-factor | 0.185 |
Rwork | 0.183 |
R-free | 0.21900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3kpf |
RMSD bond length | 0.010 |
RMSD bond angle | 1.253 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0043) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.270 |
High resolution limit [Å] | 3.200 | 3.200 |
Number of reflections | 35410 | |
<I/σ(I)> | 9.3 | 3.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.6 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 293 | 50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |