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 |
