3KPF
X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays
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 | 2009-03-05 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 138.606, 138.606, 189.471 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.900 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.22300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1b37 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.220 |
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 | 2.970 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.133 | |
Number of reflections | 45830 | |
<I/σ(I)> | 10.4 | 3 |
Completeness [%] | 96.9 | 98.1 |
Redundancy | 4 | 4 |
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 |