5EFW
Crystal structure of LOV2-Zdk1 - the complex of oat LOV2 and the affibody protein Zdark1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-06-16 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.9785 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 54.700, 54.700, 188.030 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.280 - 2.100 |
R-factor | 0.2045 |
Rwork | 0.202 |
R-free | 0.25660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2v1a 1lp1 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.064 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.200 | |
High resolution limit [Å] | 2.100 | 10.000 | 2.100 |
Rmerge | 0.104 | 0.070 | 0.528 |
Rmeas | 0.115 | 0.077 | 0.577 |
Total number of observations | 100397 | ||
Number of reflections | 17450 | 204 | 2220 |
<I/σ(I)> | 10.3 | 20.6 | 3.26 |
Completeness [%] | 99.4 | 94.9 | 100 |
Redundancy | 5.8 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 3.5 | 293.15 | 2 M ammonium sulfate, 0.1 M sodium citrate pH 3.5 |