3GDI
Mammalian Clock Protein mPER2 - Crystal Structure of a PAS Domain Fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-08-25 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97805 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.670, 63.380, 72.510 |
| Unit cell angles | 90.00, 102.25, 90.00 |
Refinement procedure
| Resolution | 19.920 - 2.400 |
| R-factor | 0.264 |
| Rwork | 0.224 |
| R-free | 0.27200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wa9 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.400 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.920 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.067 | 0.608 |
| Number of reflections | 23980 | 2742 |
| <I/σ(I)> | 17.15 | 3 |
| Completeness [%] | 98.4 | 98 |
| Redundancy | 5.77 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.7 | 298 | 23% PEG8000, 100 mM HEPES pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
