3RTY
Structure of an Enclosed Dimer Formed by The Drosophila Period Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 60.414, 94.697, 141.030 |
| Unit cell angles | 88.19, 89.63, 89.87 |
Refinement procedure
| Resolution | 20.010 - 2.850 |
| R-factor | 0.239 |
| Rwork | 0.239 |
| R-free | 0.28900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | CNS (1.3) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 30.000 |
| High resolution limit [Å] | 2.850 |
| Number of reflections | 62952 |
| <I/σ(I)> | 14.2 |
| Completeness [%] | 92.4 |
| Redundancy | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 294 | 200 mM lithium chloride, 20 % (w/v) PEG 3350, 100 mM Bicine, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
