2YR5
Crystal structure of L-phenylalanine oxidase from Psuedomonas sp.P501
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL45XU |
Synchrotron site | SPring-8 |
Beamline | BL45XU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-07-13 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 0.97200 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 101.648, 112.624, 136.609 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.620 - 1.250 |
R-factor | 0.10272 |
Rwork | 0.101 |
R-free | 0.12851 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yr4 |
RMSD bond length | 0.028 |
RMSD bond angle | 2.355 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.620 | 1.290 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmerge | 0.085 | 0.381 |
Number of reflections | 429065 | |
Completeness [%] | 97.8 | 93.4 |
Redundancy | 5.3 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 293 | 0.1M HEPES pH7.5, 1.0M ammonium sulfate, VAPOR DIFFUSION, temperature 293K |