6X1G
Crystal structure of a GEF domain from the Orientia tsutsugamushi protein OtDUB in complex with Rac1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-06-07 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.98 |
Spacegroup name | P 1 |
Unit cell lengths | 50.063, 54.160, 94.004 |
Unit cell angles | 83.37, 76.34, 62.52 |
Refinement procedure
Resolution | 48.050 - 1.600 |
R-factor | 0.1828 |
Rwork | 0.181 |
R-free | 0.21820 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1foe |
RMSD bond length | 0.014 |
RMSD bond angle | 1.808 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.630 |
High resolution limit [Å] | 1.600 | 4.340 | 1.600 |
Rmerge | 0.038 | 0.025 | 0.731 |
Rmeas | 0.053 | 0.035 | 1.033 |
Rpim | 0.038 | 0.025 | 0.731 |
Total number of observations | 151064 | ||
Number of reflections | 92107 | 4935 | 4510 |
<I/σ(I)> | 10.4 | ||
Completeness [%] | 81.7 | 87.4 | 80.2 |
Redundancy | 1.6 | 1.7 | 1.6 |
CC(1/2) | 0.996 | 0.295 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 9.5 | 293 | 25 mM CHES pH 9.5, 25% (w/v) PEG 8000 |