6IJ2
Crystal structure of a standalone versatile EAL protein from Vibrio cholerae O395 - 5'-pGpG bound form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-07-23 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.9677 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.483, 42.711, 158.470 |
Unit cell angles | 90.00, 94.94, 90.00 |
Refinement procedure
Resolution | 51.511 - 1.700 |
R-factor | 0.1837 |
Rwork | 0.182 |
R-free | 0.22020 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gfx |
RMSD bond length | 0.018 |
RMSD bond angle | 0.797 |
Data reduction software | XDS |
Data scaling software | Aimless (0.3.11) |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 52.630 | 52.630 | 1.730 |
High resolution limit [Å] | 1.700 | 9.310 | 1.700 |
Rmerge | 0.038 | 0.029 | 0.600 |
Rmeas | 0.045 | 0.037 | 0.715 |
Rpim | 0.024 | 0.023 | 0.384 |
Total number of observations | 361603 | ||
Number of reflections | 106944 | 709 | 5230 |
<I/σ(I)> | 13.8 | ||
Completeness [%] | 98.5 | 96.2 | 99.5 |
Redundancy | 3.4 | 2.9 | 3.4 |
CC(1/2) | 0.998 | 0.998 | 0.882 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | PEG 4000, sodium acetate, ammonium acetate |