7M1S
Crystal structure of human guanylate-binding protein 2 (hGBP2) K51A mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-1 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-1 |
Temperature [K] | 80 |
Detector technology | PIXEL |
Collection date | 2018-10-02 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.920126 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.631, 140.569, 240.079 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.640 - 2.910 |
R-factor | 0.2333 |
Rwork | 0.245 |
R-free | 0.27360 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dg3 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.950 |
High resolution limit [Å] | 2.900 | 7.860 | 2.900 |
Rmerge | 0.173 | 0.049 | 1.741 |
Rmeas | 0.182 | 0.052 | 1.855 |
Rpim | 0.056 | 0.017 | 0.622 |
Total number of observations | 211551 | ||
Number of reflections | 22461 | 1239 | 1098 |
<I/σ(I)> | 4.5 | ||
Completeness [%] | 99.9 | 99.8 | 98.8 |
Redundancy | 9.4 | 9.6 | 7.1 |
CC(1/2) | 0.999 | 0.708 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 289.15 | 0.7M NaH2PO4, 1.05M K2HPO4, 0.1M sodium acetate pH 3.8 |