4IV9
Structure of the Flavoprotein Tryptophan-2-Monooxygenase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2011-10-11 |
Detector | RIGAKU RAXIS HTC |
Wavelength(s) | 1.54178 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 111.135, 122.207, 76.627 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.028 - 1.951 |
R-factor | 0.1902 |
Rwork | 0.187 |
R-free | 0.24460 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yr5 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.096 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.1_1161)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 76214 | |
<I/σ(I)> | 11 | 2.1 |
Completeness [%] | 99.5 | 96.5 |
Redundancy | 5.4 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 1.6 M sodium/potassium phosphate, 12% ethylene glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |