6NQR
Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2)- Y63(3-NO2Y)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL14-1 |
Synchrotron site | SSRL |
Beamline | BL14-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-05-25 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.195 |
Spacegroup name | P 1 |
Unit cell lengths | 71.610, 79.430, 85.930 |
Unit cell angles | 89.96, 92.53, 94.76 |
Refinement procedure
Resolution | 37.510 - 2.900 |
R-factor | 0.22 |
Rwork | 0.216 |
R-free | 0.28300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4uts |
RMSD bond length | 0.010 |
RMSD bond angle | 1.346 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.13RC2_2986: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.514 | 2.980 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmeas | 0.094 | 0.880 |
Number of reflections | 36613 | 2678 |
<I/σ(I)> | 11.6 | 1.6 |
Completeness [%] | 87.5 | 86 |
Redundancy | 3.4 | 1.8 |
CC(1/2) | 0.997 | 0.597 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M Tris-HCl at pH 7.4, 0.1 M MgCl2, 16.5% PEG 3350 |