2BYV
Structure of the cAMP responsive exchange factor Epac2 in its auto- inhibited state
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 | 2004-12-14 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.406, 97.038, 172.101 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.880 - 2.700 |
| R-factor | 0.248 |
| Rwork | 0.245 |
| R-free | 0.29700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1o7f PDB ENTRY 1BKD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.950 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.060 | 0.300 |
| Number of reflections | 35428 | |
| <I/σ(I)> | 23.2 | 4.5 |
| Completeness [%] | 98.6 | 96.9 |
| Redundancy | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 100 MM BISTRISPROPANE7.5, 200 MM NANO3, 12% PEG 3350, pH 7.50 |
