Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12C |
| Synchrotron site | NSLS |
| Beamline | X12C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 103.513, 103.513, 269.727 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.230 |
| Rwork | 0.215 |
| R-free | 0.23100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDE4 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | |
| High resolution limit [Å] | 2.230 | 2.230 |
| Rmerge | 0.072 | 0.489 |
| Number of reflections | 70925 | |
| <I/σ(I)> | 27.8 | 3 |
| Redundancy | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | The protein drops contain 3 microl PDE9A2-IBMX complex and 1 microl well buffer of 0.1 M HEPES, 2.2 M Na formate, and 5% xylitol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
