4YVO
Crystal Structure of the TPR Domain of Arabidopsis FLU (FLU-TPR)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-07-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 60.193, 60.193, 67.489 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 26.064 - 1.450 |
| R-factor | 0.1421 |
| Rwork | 0.140 |
| R-free | 0.17540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ro3 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.942 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.450 |
| Number of reflections | 25072 |
| <I/σ(I)> | 24.9 |
| Completeness [%] | 98.0 |
| Redundancy | 10.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 277 | 0.2M NaCl, 0.1M Bis-tris pH6.5, 25% PEG 3350 |






