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 |