1B1C
CRYSTAL STRUCTURE OF THE FMN-BINDING DOMAIN OF HUMAN CYTOCHROME P450 REDUCTASE AT 1.93A RESOLUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 287 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.310, 51.440, 47.600 |
Unit cell angles | 90.00, 105.93, 90.00 |
Refinement procedure
Resolution | 19.450 - 1.930 |
R-factor | 0.1973 * |
Rwork | 0.197 |
R-free | 0.24300 |
Structure solution method | MIRAS |
RMSD bond length | 0.010 |
RMSD bond angle | 26.300 * |
Data reduction software | DENZO |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | RSPS |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.450 | |
High resolution limit [Å] | 1.930 | 1.930 |
Rmerge | 0.082 | 0.193 |
Number of reflections | 13289 | |
Completeness [%] | 89.2 | 72.9 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7 | 4 * | Zhao, Q., (1996) J.Struct.Biol., 116, 320. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | PEG400 | 18-20 (%(w/v)) | |
2 | 1 | 1 | HEPES | 100 (mM) | |
3 | 1 | 1 | 200 (mM) |