6K7E
Crystal structure of MBPapo-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 | CCD |
Collection date | 2017-05-21 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.9000 |
Spacegroup name | H 3 |
Unit cell lengths | 156.807, 156.807, 67.386 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.202 - 1.534 |
R-factor | 0.1667 |
Rwork | 0.166 |
R-free | 0.18930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1peb 2ciu |
RMSD bond length | 0.019 |
RMSD bond angle | 1.719 |
Data reduction software | HKL-2000 (714) |
Data scaling software | HKL-2000 (714) |
Phasing software | PHENIX (1.8_1069) |
Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.560 |
High resolution limit [Å] | 1.530 | 1.530 |
Rmerge | 0.118 | |
Number of reflections | 92372 | 4565 |
<I/σ(I)> | 8.78 | 2.3 |
Completeness [%] | 99.9 | 100 |
Redundancy | 10.2 | |
CC(1/2) | 0.691 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2M CaCl2, 0.1M HEPES, pH 7.0, 20% PEG 6000 (w/v) |