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 |