2YG6
Structure-based redesign of cofactor binding in Putrescine Oxidase: P15I-A394C double mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 198.450, 80.290, 91.430 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 51.050 - 2.500 |
R-factor | 0.18628 |
Rwork | 0.184 |
R-free | 0.23081 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yg3 |
RMSD bond length | 0.022 |
RMSD bond angle | 1.911 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CCP4 |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.100 | 0.600 |
Number of reflections | 51121 | |
<I/σ(I)> | 11.2 | 5.5 |
Completeness [%] | 99.5 | 100 |
Redundancy | 5 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.4 | pH 6.4 |