2V0W
N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal transduction (cryo-trapped light structure of LOV2 (404-546))
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 105 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 35.565, 56.021, 66.507 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 16.050 - 1.700 |
R-factor | 0.163 |
Rwork | 0.160 |
R-free | 0.21500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2v0u |
RMSD bond length | 0.016 |
RMSD bond angle | 1.553 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.043 | 0.360 |
Number of reflections | 50154 | |
<I/σ(I)> | 27 | 3.3 |
Completeness [%] | 98.0 | 93 |
Redundancy | 3.3 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | Reservoir: 0.07 M sodium acetate, pH 4.6, 5.6% PEG 4000, 30% glycerol |