6K7F
Crystal structure of MBPholo-Tim21 fusion protein with a 17-residue helical linker
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-11-02 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.970, 69.410, 171.360 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.282 - 1.800 |
R-factor | 0.1766 |
Rwork | 0.174 |
R-free | 0.21630 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1anf 2ciu |
RMSD bond length | 0.010 |
RMSD bond angle | 1.317 |
Data reduction software | XDS (Jan 26, 2018) |
Data scaling software | XDS (Jan 26, 2018) |
Phasing software | PHENIX (1.8_1069) |
Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.910 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.047 | |
Number of reflections | 46285 | 7366 |
<I/σ(I)> | 19.26 | 2.02 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 6.6 | |
CC(1/2) | 0.885 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2M K/Na Tartrate, 16% PEG 3350 (w/v), microseeds |