2VOU
Structure of 2,6-dihydroxypyridine-3-hydroxylase from Arthrobacter nicotinovorans
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-09-05 |
Detector | MARRESEARCH |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 185.960, 185.960, 104.760 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 27.920 - 2.600 |
R-factor | 0.186 |
Rwork | 0.185 |
R-free | 0.22200 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.013 |
RMSD bond angle | 1.505 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHELXD |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.800 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.070 | 0.510 |
Number of reflections | 64088 | |
<I/σ(I)> | 15 | 2.4 |
Completeness [%] | 99.7 | 99.5 |
Redundancy | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.6 | 0.1 M SODIUM CACODYLATE PH 6.6, 15% (W/V) PEG 8000, 200 MM MAGNESIUM ACETATE, 20% (V/V) GLYCEROL |