6IH1
Crystal structure of a standalone versatile EAL protein from Vibrio cholerae O395 - c-di-GMP bound form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER IMUS MICROFOCUS |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2016-04-15 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54179 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.500, 42.630, 156.340 |
Unit cell angles | 90.00, 94.42, 90.00 |
Refinement procedure
Resolution | 40.923 - 1.950 |
R-factor | 0.1852 |
Rwork | 0.183 |
R-free | 0.22170 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.054 |
Data reduction software | MOSFLM |
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] | 41.120 | 41.120 | 2.000 |
High resolution limit [Å] | 1.950 | 9.150 | 1.950 |
Rmerge | 0.052 | 0.024 | 0.327 |
Rmeas | 0.072 | 0.034 | 0.454 |
Rpim | 0.049 | 0.024 | 0.315 |
Total number of observations | 126224 | 1215 | 8135 |
Number of reflections | 68489 | 663 | 4400 |
<I/σ(I)> | 6 | 11.3 | 1.7 |
Completeness [%] | 96.5 | 90.1 | 93.8 |
Redundancy | 1.8 | 1.8 | 1.8 |
CC(1/2) | 0.997 | 0.997 | 0.763 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | PEG 4000, ammonium acetate, sodium citrate |