3IBJ
X-ray structure of PDE2A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-10-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.28 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.233, 89.699, 264.187 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.260 - 3.020 |
| R-factor | 0.2147 |
| Rwork | 0.210 |
| R-free | 0.31100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1MC0; 1Z1L |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.381 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | BUSTER-TNT (2.1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.141 | |
| Number of reflections | 31809 | |
| <I/σ(I)> | 28.57 | |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 14.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 277 | Purified PDE2(215-900) was exchanged into crystallization buffer (50 mM HEPES pH7.5, 50 mM NaCl, and 2 mM TCEP) to a final concentration of 10mg/ml. Protein was mixed 1:1 with precipitant solution composed of 5-10% isopropanol, 0.1 M MES pH5.4-6.0, 0.2M Ca(OAc)2. Clusters of thin plate-like crystals appeared in 3-4 days, VAPOR DIFFUSION, temperature 277K |
