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 |