1FAH
STRUCTURE OF CYTOCHROME P450
Experimental procedure
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 296 |
Detector technology | AREA DETECTOR |
Collection date | 1994-09-19 |
Detector | SIEMENS-NICOLET X100 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.500, 154.000, 62.400 |
Unit cell angles | 90.00, 95.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.300 |
R-factor | 0.172 |
Rwork | 0.172 |
Structure solution method | DIFFERENCE FOURIER |
Starting model (for MR) | WILD TYPE P450BM-3 HEME DOMAIN |
RMSD bond length | 0.008 |
RMSD bond angle | 23.100 * |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.080 | 0.300 |
Total number of observations | 120931 * | |
Number of reflections | 44522 | |
<I/σ(I)> | 10.39 | 1 |
Completeness [%] | 88.2 | 62.5 * |
Redundancy | 3 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.8 | SEE REFERENCE 1, pH 6.8 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 40 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 16 (%) | |
3 | 1 | reservoir | 100 (mM) | ||
4 | 1 | reservoir | PIPES | 100 (mM) |