1W1J
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-11-15 |
Detector | MARRESEARCH |
Spacegroup name | I 4 |
Unit cell lengths | 129.519, 129.519, 133.280 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.700 |
R-factor | 0.211 |
Rwork | 0.207 |
R-free | 0.29200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vao |
RMSD bond length | 0.014 |
RMSD bond angle | 1.504 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CCP4 |
Refinement software | REFMAC (5.1.27) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.075 | 0.341 |
Number of reflections | 28016 | |
<I/σ(I)> | 3 | |
Completeness [%] | 97.9 | 97.6 |
Redundancy | 2.1 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6 |