1LQ9
Crystal Structure of a Monooxygenase from the Gene ActVA-Orf6 of Streptomyces coelicolor Strain A3(2)
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 |
Collection date | 2000-10-04 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9326 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.028, 60.168, 71.379 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.300 |
Rwork | 0.142 |
R-free | 0.16800 |
Structure solution method | MIRAS |
RMSD bond length | 0.013 * |
RMSD bond angle | 0.990 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.320 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.059 | 0.136 |
Total number of observations | 798091 * | |
Number of reflections | 50368 * | |
<I/σ(I)> | 12.2 | |
Completeness [%] | 99.8 * | 100 |
Redundancy | 15.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 293 | ammonium sulfate, PEG 200, Tris or Hepes buffer, pH 7.0, VAPOR DIFFUSION, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 1.5 (M) | |
2 | 1 | reservoir | HEPES | 100 (mM) | pH7.0 |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.0 |
4 | 1 | reservoir | PEG200 | 10-15 (%) |