3B99
Crystal structure of zebrafish prostacyclin synthase (cytochrome P450 8A1) in complex with substrate analog U51605
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-07 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 58.470, 88.044, 190.142 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.750 - 2.500 |
| R-factor | 0.218 |
| Rwork | 0.214 |
| R-free | 0.29209 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2iag |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.404 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 32622 | |
| <I/σ(I)> | 12.9 | 2.8 |
| Completeness [%] | 92.3 | 94.2 |
| Redundancy | 4.7 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Soaking | 7.5 | 277 | The crystal of prostacyclin synthase-U51605 complex was prepared by soaking the ligand-free crystals in 2 microliter of substitute mother liquor (23% PEG 3350, 50mM HEPES (Na-salt; pH 7.5)) containing 0.25mM of U51605 for a week, Soaking, temperature 277K |
