2E46
Crystal Structure Analysis of the clock protein EA4
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-06-08 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 59.500, 59.500, 112.072 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.760 - 2.300 |
| R-factor | 0.21229 |
| Rwork | 0.208 |
| R-free | 0.28522 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e9p |
| RMSD bond length | 0.036 |
| RMSD bond angle | 2.902 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 2.300 |
| Number of reflections | 9519 |
| Completeness [%] | 99.9 |
| Redundancy | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 293 | 9% ethlene glycol, 1M ammonium fluoride, 100mM Bis-Tris, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






