2E47
Crystal Structure Analysis of the clock protein EA4 (glycosylation form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
| Synchrotron site | Photon Factory |
| Beamline | AR-NW12A |
| Collection date | 2005-02-02 |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.098, 73.894, 47.446 |
| Unit cell angles | 90.00, 104.07, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.110 |
| R-factor | 0.17425 |
| Rwork | 0.170 |
| R-free | 0.25110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e9p |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.066 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 17500 | |
| Completeness [%] | 95.5 | |
| Redundancy | 4.1 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 27% PEG 3350, 500mM magnesium chloride, 20mM sodium fluoride, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
