1EHG
CRYSTAL STRUCTURES OF CYTOCHROME P450NOR AND ITS MUTANTS (SER286 VAL, THR) IN THE FERRIC RESTING STATE AT CRYOGENIC TEMPERATURE: A COMPARATIVE ANALYSIS WITH MONOOXYGENASE CYTOCHROME P450S
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-06-29 |
| Detector | RIGAKU RAXIS |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.751, 81.860, 85.720 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.700 |
| R-factor | 0.193 |
| Rwork | 0.193 |
| R-free | 0.22300 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.230 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.070 | 0.257 |
| Number of reflections | 41636 | |
| <I/σ(I)> | 7.8 | |
| Completeness [%] | 96.8 | 88.7 |
| Redundancy | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 * | 293 | protein was crystallized from 100mM-Mes buffer, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | potassium phosphate | 1 (mM) | |
| 3 | 1 | drop | glycerol | 10 (%(v/v)) | |
| 4 | 1 | drop | dithiothreitol | 0.1 (mM) | |
| 5 | 1 | drop | EDTA | 0.1 (mM) | |
| 6 | 1 | reservoir | PEG4000 | 36 (%) | |
| 7 | 1 | reservoir | MES | 100 (mM) | |
| 8 | 1 | reservoir | glycerol | 10 (%) |
