4CY8
2-hydroxybiphenyl 3-monooxygenase (HbpA) in complex with FAD
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04-1 |
Synchrotron site | Diamond |
Beamline | I04-1 |
Temperature [K] | 120 |
Detector technology | PIXEL |
Collection date | 2013-12-12 |
Detector | DECTRIS PILATUS 2M |
Spacegroup name | P 1 |
Unit cell lengths | 80.000, 96.180, 102.160 |
Unit cell angles | 114.09, 95.80, 109.31 |
Refinement procedure
Resolution | 59.530 - 2.030 |
R-factor | 0.17109 |
Rwork | 0.169 |
R-free | 0.20246 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ihg |
RMSD bond length | 0.016 |
RMSD bond angle | 1.749 |
Data reduction software | xia2 |
Data scaling software | SCALA |
Phasing software | BALBES |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 59.530 | 2.080 |
High resolution limit [Å] | 2.030 | 2.030 |
Rmerge | 0.070 | 0.430 |
Number of reflections | 146673 | |
<I/σ(I)> | 5.4 | 2.1 |
Completeness [%] | 90.0 | 92 |
Redundancy | 2.3 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | 18% (W/V) PEG 3350, 0.15 M KSCN, 1 MM FAD IN BIS-TRIS PROPANE BUFFER AT PH 5.5, WITH A PROTEIN CONCENTRATION OF 10 MG ML-1 |